ID A0A494YUZ0_9BACI Unreviewed; 499 AA.
AC A0A494YUZ0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 03-MAY-2023, entry version 8.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=D8M05_14625 {ECO:0000313|EMBL:RKQ13918.1};
OS Oceanobacillus bengalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=1435466 {ECO:0000313|EMBL:RKQ13918.1, ECO:0000313|Proteomes:UP000281813};
RN [1] {ECO:0000313|EMBL:RKQ13918.1, ECO:0000313|Proteomes:UP000281813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1K00260 {ECO:0000313|EMBL:RKQ13918.1,
RC ECO:0000313|Proteomes:UP000281813};
RX PubMed=26303283; DOI=10.1007/s10482-015-0573-5;
RA Yongchang O., Xiang W., Wang G.;
RT "Oceanobacillus bengalensis sp. nov., a bacterium isolated from seawater of
RT the Bay of Bengal.";
RL Antonie Van Leeuwenhoek 108:1189-1196(2015).
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC -!- SIMILARITY: Belongs to the peptidase M32 family.
CC {ECO:0000256|PIRNR:PIRNR006615}.
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:RKQ13918.1}.
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DR EMBL; RBZO01000025; RKQ13918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494YUZ0; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000281813; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd06460; M32_Taq; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:RKQ13918.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Reference proteome {ECO:0000313|Proteomes:UP000281813};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 265
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 499 AA; 57941 MW; FEF179AB560F86B6 CRC64;
MENIKSIEKE FIDLLHEIDA YREVITLTQW DLRTKIPPKG VEQRSEVVGV LSEKVHQLET
SEKMKQYIDA LKNKTEDKII QKAVETCEET YNRSSKIPIA EFKEYVMVQS KSEAIWQEAR
EKADFSLFQP YLEKLVDFNK KFANYWGYKD NIYDALLHNF EPGMTTKILD EVFSKLRQAL
TGLLSKINAS TTKPDSSVLI GHFPKSNQEA FTVEVLKQMG YDFESGRLDE TIHPFEITLN
MNDVRITTRY DEEDFRMAVF GTIHEGGHAL YEQNISPKLA RTPLATGTSM GIHESQSLFW
ENFVSRSKAF WGNNYDLLKS YAPDAFEHVT LEDFYCAINE VKPSFIRIEA DELTYALHIM
IRYELEKGLM NGEMEVKDLP QLWNEKMEDY LGIKPPTDKE GVLQDIHWAG GDFGYFPSYA
LGYMYAAQFH HTMKKELNVD QLIASGDLAP IKEWLTKHIH QYGKMKKPLE IIEDVTEEKL
NSDYLVQYLT EKYTDIYGL
//