ID   D9WAQ7_9ACTN            Unreviewed;       993 AA.
AC   D9WAQ7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Putative zinc-binding carboxypeptidase {ECO:0000313|EMBL:EFL26998.1};
GN   ORFNames=SSOG_06712 {ECO:0000313|EMBL:EFL26998.1};
OS   Streptomyces himastatinicus ATCC 53653.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL26998.1, ECO:0000313|Proteomes:UP000003963};
RN   [1] {ECO:0000313|EMBL:EFL26998.1, ECO:0000313|Proteomes:UP000003963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL26998.1,
RC   ECO:0000313|Proteomes:UP000003963};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; GG657754; EFL26998.1; -; Genomic_DNA.
DR   RefSeq; WP_009718798.1; NZ_GG657754.1.
DR   AlphaFoldDB; D9WAQ7; -.
DR   STRING; 457427.SSOG_06712; -.
DR   HOGENOM; CLU_012481_0_0_11; -.
DR   OrthoDB; 5240362at2; -.
DR   Proteomes; UP000003963; Unassembled WGS sequence.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd03859; M14_CPT; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR033810; Carboxypeptidase_T.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   PANTHER; PTHR11705:SF145; SLL0236 PROTEIN; 1.
DR   Pfam; PF20773; InhA-like_MAM; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:EFL26998.1};
KW   Hydrolase {ECO:0000313|EMBL:EFL26998.1};
KW   Protease {ECO:0000313|EMBL:EFL26998.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..993
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003131069"
FT   DOMAIN          181..203
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   REGION          281..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   993 AA;  105896 MW;  E6541CD1ACC8FF5D CRC64;
     MKTRKAGWRR TARAVGSAAA LASLLLTGLA ATPAAHAQPA AGTAGETITV WTAQVTRAQI
     PLLLRAGVDG TELGTQVPEK GAGTVELYLT GTQAAALRGQ GVALTEKKLS QRTLSRVKAA
     GDGVFRPYSG DGGLRQEIVE TGQAHPGLTK VVSIGKTTQG KDILALKLTK GAAKSRDGSK
     PSVLYMSNQH AREWITPEMT RRLMHYYLDN YGKDHRVTRI VDRSELWFVL SANPDGYDYT
     HQSPANRQWR KTLRDNNGDG KITPGDGVDP NRNFPYKWGY DNEGSSADPA DETYRGPAPG
     SEPETKALDR FQKRIGFAYG INYHSAAELL LYGVGWQVAT PTPDDVLYKA LAGTPEHSAI
     PGYHPQVSSE LYTTNGEADG HAANVNGMMM FTPEMSTCQT ASNVDPNDAW QPRDCASGFT
     FPDDEKLIQQ EFAKNVPFAL SVAETARHPD QPSSSVGMTA PDFTPDAFTA SYARGAAQDV
     SVTARKSVRA KTLAYRVNGG RTHTASLRPW KGGETYGGED NIHFDQYRAA VRGADPGDTV
     KVWFTGRTED GERTASEPFT YTVAERPRAD TLVIAEEGGD APPRHLAAYT DALARNGRKA
     AVWDVATQGA PSALGVLGHF RTVLWYTGAQ KPGGATLLAV RDYLNEGGKL ITTGEQTGGS
     SLVGPADTDD FSQYYLGADS RLTVQSPPAY QGAGALDGTS ATLGDAPGNP LDAAGAYTVT
     SDVLPPEDFP QFRSAGAGAY SGARTPYEPY EGEWMAAAVH RNSSWARLSR TVDLTGVDAG
     DEPSLTFRLS YDTEPGYDHV IAEAHTVGKD DWTTLPDAGG ASSDRVPAEC EAGFLLTTHP
     FLKRYLTAAD DGCRAEGGTG AWNSFTGSSG GWKPVTLDLS RYAGEKVELA LSYVTDSSVG
     GRGAFVDSTA LVTGGDTRDA EGFETALGPW SVPGPPEGSP ANAADWTRSK ELFRTAAAVT
     TRDTVLLGYG LEHVRDAAQR ASLVRSALRA LRR
//