ID Q836G0_ENTFA Unreviewed; 498 AA.
AC Q836G0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN OrderedLocusNames=EF_1153 {ECO:0000313|EMBL:AAO80953.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO80953.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO80953.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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}.
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DR EMBL; AE016830; AAO80953.1; -; Genomic_DNA.
DR RefSeq; NP_814883.1; NC_004668.1.
DR RefSeq; WP_002379331.1; NZ_KE136528.1.
DR AlphaFoldDB; Q836G0; -.
DR STRING; 226185.EF_1153; -.
DR EnsemblBacteria; AAO80953; AAO80953; EF_1153.
DR KEGG; efa:EF1153; -.
DR PATRIC; fig|226185.45.peg.2343; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_1_9; -.
DR Proteomes; UP000001415; Chromosome.
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:AAO80953.1}; 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:UP000001415};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 263
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 498 AA; 57684 MW; 6489BB7DCC78704A CRC64;
MKEAVFLQEV KEIQLLKNAL TLLDWDSSTG MPEKSSPFRG EVEGYLTGLY FERSIGPVIQ
EALAYFETRP EELSELGKLV FEKVKEEYAL NKNVPAERMQ EYVKVLNQAH TDWLKARAAQ
DFGLLEETLT KVVAFQKEFI PYWQKEEKTP YDVLLNQFEP GMTVEKLDQV FDQVKQGIQE
IRTVLAEKGT PPRTDFLSRK MTKEQQRRFV IGVVEQLGYD FSKGRLDDTV HPFMTALNRN
DARITTRWEE NNFSMATFGV IHEAGHGMYE QNFDPKFDFT PLSEGASMGI HESQSLFNEI
IIGSNRAFWQ KQYPFFQECA EGTFDDIAFE DFYASLKETK ASLIRIDSDS LTYPLHIIIR
YEIEKMLFNG SLEVADLPKV WNEKYQEYLG VSPENDLEGA LQDVHWSGGS FGYFPSYALG
YMYAAQLFHA MKQELSVDEI LASEDYSDIR KWLTQHIHQY GASRKPNQLI YDATGEELNP
SYLIDYMKAI YFDVYQVQ
//
