ID   A0A0S7YKL9_9BACT        Unreviewed;       506 AA.
AC   A0A0S7YKL9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=AMS19_14560 {ECO:0000313|EMBL:KPJ74987.1};
OS   Gemmatimonas sp. SG8_23.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703356 {ECO:0000313|EMBL:KPJ74987.1, ECO:0000313|Proteomes:UP000051174};
RN   [1] {ECO:0000313|EMBL:KPJ74987.1, ECO:0000313|Proteomes:UP000051174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_23 {ECO:0000313|EMBL:KPJ74987.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC       sequentially from the C-terminus, including neutral, aromatic, polar
CC       and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity,
CC         except for -Pro.; EC=3.4.17.19;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC   -!- SIMILARITY: Belongs to the peptidase M32 family.
CC       {ECO:0000256|PIRNR:PIRNR006615}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPJ74987.1}.
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DR   EMBL; LJNO01000291; KPJ74987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7YKL9; -.
DR   PATRIC; fig|1703356.3.peg.2096; -.
DR   Proteomes; UP000051174; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd06460; M32_Taq; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02074; Peptidase_M32; 1.
DR   PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR   PRINTS; PR00998; CRBOXYPTASET.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000313|EMBL:KPJ74987.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000256|PIRSR:PIRSR006615-1};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW   Protease {ECO:0000256|PIRNR:PIRNR006615};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        263
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   506 AA;  57505 MW;  1B5ABD75CBA81C80 CRC64;
     MGYNELLVRM GEVNDLLCSE SMLSWDERTM MPPGGAVTRG KQLATLKVFA RNHLVSAETR
     RLLDAAEAET ASLAEDSVER TICAHVREAI DYHTRIPAEL VQRRAELGSR GQHVWAKARQ
     ESDYASFAPI LEETLELNRE MAECIGYEEH PYDALMYRFE PGETLASLQP LFAALREGLL
     PLVRAIAEKE PPRVDFLQRP FPVDRQLAFA LSMARKVGYD TNRGRLDLTV HPFEISFTRN
     DVRITTRVND EWMPKSLFGT LHEAGHGMYE QYCDPAYTRT PLATDLVGLY AVGGVSFGAH
     ESQSRLFENQ VGRSREFWDL NYGELHDAFP EQLAGIDVET FWRAVNRVQP GFIRVESDEL
     TYDFHIMLRV DIEAALIDGS LSVADLPEAW NAKVEEYLGL DVPNDRLGVL QDVHWSSGQV
     GTFCNYTIGN VMAGQLFAEA KKDDRVRDGL AAAEYGPLRE WMTEHVHRHG RRYTREQLLE
     RSTGRGLDPT DYVAYLTDKY TEVYEL
//