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Database: UniProt
Entry: A0A2W7I7N8_9FLAO
LinkDB: A0A2W7I7N8_9FLAO
Original site: A0A2W7I7N8_9FLAO 
ID   A0A2W7I7N8_9FLAO        Unreviewed;       380 AA.
AC   A0A2W7I7N8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:PZW42674.1};
GN   ORFNames=LX95_00990 {ECO:0000313|EMBL:PZW42674.1};
OS   Mesonia algae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mesonia.
OX   NCBI_TaxID=213248 {ECO:0000313|EMBL:PZW42674.1, ECO:0000313|Proteomes:UP000249542};
RN   [1] {ECO:0000313|EMBL:PZW42674.1, ECO:0000313|Proteomes:UP000249542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15361 {ECO:0000313|EMBL:PZW42674.1,
RC   ECO:0000313|Proteomes:UP000249542};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) 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}.
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:PZW42674.1}.
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DR   EMBL; QKYV01000002; PZW42674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7I7N8; -.
DR   Proteomes; UP000249542; 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; cd06239; M14-like; 1.
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:PZW42674.1};
KW   Hydrolase {ECO:0000313|EMBL:PZW42674.1};
KW   Protease {ECO:0000313|EMBL:PZW42674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249542}.
FT   DOMAIN          22..254
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   380 AA;  43389 MW;  391B769C2000FA57 CRC64;
     MEINKLLDIA GTYRNTSFLG RYISQETIDS FINTFPETHK SIIGTSVEKR PITQLKLGEG
     SIKVLMWSQM HGNETTTTKA LIDFIGFLQS NSAEAKEILS QISFTIIPQL NPDGAKAYTR
     VNKNAVDLNR DAQDCTQPES RAFKKVYKEL QPHFCFNLHD QRTIFGVGKP AKPATVSFLS
     PAFNDSRALN DTREKAMKLI VYMNQSLQET IPNQVGRYDD GFNLNCVGDT LQNLGFPTIL
     FEAGHFQNDY QRAETRKFIF ISLLKGIWGI IKNKYEDVDY RDYFKIPENE KCFYDILIKN
     IGNREDSLAI QYKEVLKDNK LIFLPFLVKE IGKKFTYGHH EIDAKGAILT INSILDFSKI
     TEIQEISLDG KKFSLNLTKT
//
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