ID   A0A0S8G3K3_9BACT        Unreviewed;       499 AA.
AC   A0A0S8G3K3;
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=AMS21_02380 {ECO:0000313|EMBL:KPK66461.1};
OS   Gemmatimonas sp. SG8_38_2.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703358 {ECO:0000313|EMBL:KPK66461.1, ECO:0000313|Proteomes:UP000051763};
RN   [1] {ECO:0000313|EMBL:KPK66461.1, ECO:0000313|Proteomes:UP000051763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_38_2 {ECO:0000313|EMBL:KPK66461.1};
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:KPK66461.1}.
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DR   EMBL; LJTP01000007; KPK66461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8G3K3; -.
DR   PATRIC; fig|1703358.3.peg.1471; -.
DR   Proteomes; UP000051763; 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   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        264
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   499 AA;  55937 MW;  5D3A59D9D2BABBA0 CRC64;
     MSAYETLEHR FRDISHLEHV QAMLFWDEAT MMPMGGGPAR AEALAALAGV LHERRAAPEL
     GDLLADADAS QDGLAPWQRA NLHQMRRNWR QATALPADLV TASQLAATTC EQTWRRCRPE
     QDWATVEPLL KNVIRLNREV AVRLGELEGL APYEALMDSY EEGLRTAFVE EKFRDLRDFL
     PGFLDQVLER QARAPGLALE GPFPVERQKG LGMALIKALG FNFEHGRIDV SHHPFCGGVP
     DDTRITTRYN ERDFLSALMA ALHETGHALY QQGLPDDWRG QPVGEALGMA MHESQSLLME
     MQVCRSKAFL DFAGDSIRNA FDAGTDDPAW SNSNLYKLCT KVERGFIRVD ADEVTYPLHI
     ILRFEIERKL CSGEMDVEEI PEAWNEAMRD LLGLSTAGNL RDGCMQDVHW FAGLLGYFPS
     YTLGALTAAQ LFSAARNRVD GLEQLIARGD FRPLLEWLRT HVHGRGRLKT APELLKDVTG
     APLGTEAFKS HLQSRYLAD
//