ID   A0A265N6H1_9BACI        Unreviewed;       348 AA.
AC   A0A265N6H1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:OZU87608.1};
GN   ORFNames=CIL03_16090 {ECO:0000313|EMBL:OZU87608.1};
OS   Virgibacillus indicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=2024554 {ECO:0000313|EMBL:OZU87608.1, ECO:0000313|Proteomes:UP000216498};
RN   [1] {ECO:0000313|EMBL:OZU87608.1, ECO:0000313|Proteomes:UP000216498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IO3-P2-C2 {ECO:0000313|EMBL:OZU87608.1,
RC   ECO:0000313|Proteomes:UP000216498};
RA   Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT   "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT   moderately halophilic bacteria isolated from marine sediment by using the
RT   Microfluidic Streak Plate.";
RL   Submitted (AUG-2017) 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:OZU87608.1}.
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DR   EMBL; NPMS01000009; OZU87608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A265N6H1; -.
DR   OrthoDB; 5294005at2; -.
DR   Proteomes; UP000216498; 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.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:OZU87608.1};
KW   Hydrolase {ECO:0000313|EMBL:OZU87608.1};
KW   Protease {ECO:0000313|EMBL:OZU87608.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216498};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..348
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038487280"
FT   DOMAIN          92..114
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   348 AA;  38438 MW;  408FD7FE8AFF27E9 CRC64;
     MKKQLVSIAL TGTILAGGSF ADMAFVQAAG NGPDYQGHET INTSILHTYS EMVDYLEKQE
     KKQTYMELEV IGKTVKGRDM HLVKYMQNPK NPTILYITQQ HGDEALTTEG ALDFIKQLGT
     GKTKGILENV NILFIPMYNA DGAMGDVNYE LEDYAASGDR HLTRLNANGA DLNRDHEEKT
     QPETQALHNN VLQKYDIDYM IDLHHQGAQW VKDGKYVSGA IFPSHPDHTA PEVLQGSKQL
     GAVVYDAIEP KGWGHLANYA GKGSAYDNGI SVYGLAHDYG ISTLLFEMRG TADNANDFEV
     LGQKSNGYLK KQAVIAMDSA ARAVADGTIN EKDISFWDDL PVQEERPY
//