ID   A0A1G9WEF8_9FLAO        Unreviewed;       821 AA.
AC   A0A1G9WEF8;
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:SDM82932.1};
GN   ORFNames=SAMN04488514_11577 {ECO:0000313|EMBL:SDM82932.1};
OS   Kriegella aquimaris.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kriegella.
OX   NCBI_TaxID=192904 {ECO:0000313|EMBL:SDM82932.1, ECO:0000313|Proteomes:UP000199440};
RN   [1] {ECO:0000313|EMBL:SDM82932.1, ECO:0000313|Proteomes:UP000199440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19886 {ECO:0000313|EMBL:SDM82932.1,
RC   ECO:0000313|Proteomes:UP000199440};
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; FNGV01000015; SDM82932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9WEF8; -.
DR   STRING; 192904.SAMN04488514_11577; -.
DR   OrthoDB; 9758209at2; -.
DR   Proteomes; UP000199440; 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; cd01653; GATase1; 1.
DR   CDD; cd06238; M14-like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
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; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SDM82932.1};
KW   Hydrolase {ECO:0000313|EMBL:SDM82932.1};
KW   Protease {ECO:0000313|EMBL:SDM82932.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199440};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..821
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011793309"
FT   DOMAIN          37..301
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   821 AA;  94005 MW;  CC7D772E73A3EC66 CRC64;
     MKWILLPMML LISLTSTAQQ ALQSPSEFLG YELGTQFTRH HEVVDYFKQL SEARPDQVVF
     IEYGKTYERR PLFIVYFSSA DNIKNIEKIR QTHLKSIRGE NNSEKAIVWL SYNVHGNEAS
     STEASMQTIF ELLTNKSEYL KNTVVVMDPC SNPDGRDRYV NWYNQYKNTP NNIDPESKEH
     QEGWWNGRSN HYMFDLNRDW AWLTQLESQQ RLNIYNQWLP HVHVDFHEQG VDSPYYFAPA
     AEPFHEVITD FQRNFQVTIG KNHAKYFDAN GWFYFTKEVY DLLYPSYGDT YPTYNGSIGM
     TYEQGGGGRA GLGIINGLGD TLTLNDRIEH HRITGLSTLE VVAKNTKTLN EEFVKFHQDK
     NYKYKSYVLK GNNDNTDALR RLLEQHQIEY GKATQTNIKG FDYDSGKSGN FKIDTTHVVI
     STNQPKGTLV KVLFEPNAKL SDSLTYDITA WSLPYAYGLN AIASETNIAS RPFYNRTVVQ
     EKKSNLSNDT YAFLAKWKSI KDAQFLAELL KEDIRVRYTK EPFVLDNQTY DRGSLIITRA
     DNVNKSDFVK RLNDISNKHR IVLTPTRTGF VDKGKDFGSK NVKAIKPVKI AVLSEKPTSS
     LHFGEIWHFF EQQLNYPITV LDSDNLLQTD LTKYDVLIFP GGDGYKEFLD KDELENLTNW
     IKNGGKLVAM GGALKGLSDQ KAFSLKKKIV KSDSIINMTS FDISQREGIK NLITGAIFKT
     AVDKTHPLAF GYDKTYFTLK MGNDAYQYLE NGSVVYLEKK DRNPVAGFAG STAMEKIGET
     LVFGVERHGN GQIVYMVDNP LFRGFWENGK LFFANALFLV D
//