ID   A0A1G9N3Y3_9PSED        Unreviewed;       422 AA.
AC   A0A1G9N3Y3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:SDL80817.1};
GN   ORFNames=SAMN05216186_13136 {ECO:0000313|EMBL:SDL80817.1};
OS   Pseudomonas indica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=137658 {ECO:0000313|EMBL:SDL80817.1, ECO:0000313|Proteomes:UP000198706};
RN   [1] {ECO:0000313|EMBL:SDL80817.1, ECO:0000313|Proteomes:UP000198706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21544 {ECO:0000313|EMBL:SDL80817.1,
RC   ECO:0000313|Proteomes:UP000198706};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNFD01000031; SDL80817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9N3Y3; -.
DR   STRING; 137658.SAMN05216186_13136; -.
DR   Proteomes; UP000198706; 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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SDL80817.1};
KW   Hydrolase {ECO:0000313|EMBL:SDL80817.1};
KW   Protease {ECO:0000313|EMBL:SDL80817.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198706};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..422
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011770392"
FT   DOMAIN          40..289
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   422 AA;  45732 MW;  F7B5CBC3CB10CA5C CRC64;
     MRLPIAAFLL GAGLLPGIAA AAEPNGPWVN DEQNVSLEGF MSNEQLYDQL AALARRSKGV
     LALEQIGTSG KGRPIWLARL GAADKPTVMI MTQQHGNEPH GTEAALDLIR KLATGGTFSR
     QVLDHVQVLF IPRVNPDGTA LFTRGNADFS APETSASCLK TDGTVDPAKL NQGLGSNVTA
     YTDADGQRDW SYDINRYHWP DWSQSTQILC NPGLADQRHF NPGQNPVPEA TAVRTAYDRY
     QPIWLVDVHN QNPAVVLEDA DPDINRPDRQ VTGSITWPAN DDVAQVAVDL SKQMSVVMKR
     RSMELGNMEI TNYFYQYPDG SIRRGGGEPG IARNAYALLG TQRLNSGASG PLGGSVLMEI
     TGLNSRGQKS IGMLRNNVRE MLEALLLASA DGSLYAIDPA EADRILPPGQ ETDQPLSNPH
     DE
//