ID   A0A2S5GD58_9BACL        Unreviewed;       346 AA.
AC   A0A2S5GD58;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:PPA70855.1};
GN   ORFNames=C4B60_08685 {ECO:0000313|EMBL:PPA70855.1};
OS   Jeotgalibacillus proteolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=2082395 {ECO:0000313|EMBL:PPA70855.1, ECO:0000313|Proteomes:UP000239047};
RN   [1] {ECO:0000313|EMBL:PPA70855.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22-7 {ECO:0000313|EMBL:PPA70855.1};
RA   Li Y.;
RT   "Jeotgalibacillus proteolyticum sp. nov. a protease producing bacterium
RT   isolated from ocean sediments of Laizhou Bay.";
RL   Submitted (FEB-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:PPA70855.1}.
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DR   EMBL; PREZ01000003; PPA70855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5GD58; -.
DR   OrthoDB; 9758209at2; -.
DR   Proteomes; UP000239047; 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:PPA70855.1};
KW   Hydrolase {ECO:0000313|EMBL:PPA70855.1};
KW   Protease {ECO:0000313|EMBL:PPA70855.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..346
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015772403"
FT   DOMAIN          92..114
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   346 AA;  37892 MW;  CBE3D119850B90E5 CRC64;
     MKKTLLTLSI AGAMVLSASP LATTPASAVG NGPGYGGNET INTSILHTYD EMVSYLKTQE
     AKQKDLELEV IGQSVKGRDL YLAKYMKNPD NPTILFLTQQ HGNEQLTTEG ALEFIKHLGT
     GKMKGVADNV NILIVPMLNA DGAMGDVDFS LDDYIADGGR NLTRFNAVEV DLNRDHVDKI
     QPETQALHFN VMQKYDIDYM IDLHHQGANS ERDGKLVSGS ILYPNTPNAD PEVVEKSKQL
     GAVVFDAVDS KGWGHLGKYV GGSAETISRN GIAVEYGIST LLFEMRGMSD HYREDYVLGQ
     KSNGYLIKQT ITTLDSTVRA IADGSIETMD TSFWDTLAEQ TTRQTE
//