ID   PEPVL_STAES             Reviewed;         469 AA.
AC   Q8CNV2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative dipeptidase SE_1424;
DE            EC=3.4.13.-;
GN   OrderedLocusNames=SE_1424;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO05023.1; -; Genomic_DNA.
DR   RefSeq; NP_764979.1; NC_004461.1.
DR   RefSeq; WP_002484963.1; NZ_WBME01000009.1.
DR   AlphaFoldDB; Q8CNV2; -.
DR   SMR; Q8CNV2; -.
DR   STRING; 176280.SE_1424; -.
DR   PRIDE; Q8CNV2; -.
DR   EnsemblBacteria; AAO05023; AAO05023; SE_1424.
DR   KEGG; sep:SE_1424; -.
DR   PATRIC; fig|176280.10.peg.1390; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   OMA; GYAGHIE; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01887; dipeptidaselike; 1.
PE   3: Inferred from homology;
KW   Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..469
FT                   /note="Putative dipeptidase SE_1424"
FT                   /id="PRO_0000282635"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  52759 MW;  324B560CD778EC79 CRC64;
     MWKEKVLEYE NQMIEDLKGL LSIESIRDDS KATADAPVGP GPREALDYMY NLGKRDGFST
     HDVDHIAGRI EAGKGEDVLG ILCHVDVVPA GDGWDSNPFQ PVVTDNAIIA RGTLDDKGPT
     IAAYYAVKIL NEMKVDWKKR IHIIIGTDEE SDWKCTDRYF KTEEMPALGF APDAEFPAIH
     GEKGITTFDL VQNEVTEDTD EPDYELLKFE SGQRYNMVPD YAKAEVLVKE NMTDVIQNFE
     NFLQQNQLQG ESTVDSGILI LTIEGKAVHG MDPSLGVNAG LFLLKFLASL NLNKSAKDFV
     EFNERYLFES HFGEKMGMKF HTDIMGDVTT NIGVISYDKE KAGRYGINLR YPEGFKFEDA
     IDRFRSEINE LGFNLELGKV QKPHYVDKND PFVKTLVNAY RNQTGDMTEP YTIGGGTYAR
     NLDKGVAFGA MFADSEDLMH QKNEYITKKQ LINATSIYLE AIYALCVED