ID   PEPVL_STAHJ             Reviewed;         469 AA.
AC   Q4L795;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Putative dipeptidase SH1171;
DE            EC=3.4.13.-;
GN   OrderedLocusNames=SH1171;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04480.1; -; Genomic_DNA.
DR   RefSeq; WP_011275472.1; NC_007168.1.
DR   AlphaFoldDB; Q4L795; -.
DR   SMR; Q4L795; -.
DR   STRING; 279808.SH1171; -.
DR   EnsemblBacteria; BAE04480; BAE04480; SH1171.
DR   GeneID; 58062627; -.
DR   KEGG; sha:SH1171; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   OMA; GYAGHIE; -.
DR   OrthoDB; 906744at2; -.
DR   Proteomes; UP000000543; 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 SH1171"
FT                   /id="PRO_0000282636"
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;  52904 MW;  754DBAA6B6DCA953 CRC64;
     MWKEKVQEYE GQIIDDLKGL LSIESVRDDS KASDETPVGP GPRQALDYMY EIAQRDGFST
     HDVDHIAGRI EAGKGDDVLG VLCHVDVVPA GDGWDSDPFN PVVTDDAIIA RGTLDDKGPT
     IAAYYAVKIL NDMKVDWKKR IHIIIGTDEE SDWKCTERYF QTEEMPTLGF APDAEFPAIH
     GEKGITTFDL VQNSTSEDQD EPDYELISFE SGQRYNMVPD HAQARVFVKE NMTDVVQHFE
     HYLDQHKLQG ESVVDSGELV LTLEGKAVHG MDPSLGVNAG LYLLDFISTL NLNQTAREFV
     DFSNRYLHES HFGEKMGMKF HTDVMGDVTT NVGIISYDNK QGGRFGINLR YPQKFEFEEA
     IQRFTKEIKA YGFDLELGKV QQPHFVDKND PFVQKLVKAY RNQTGDMSEP YTIGGGTYAR
     NLDKGVAFGA MFEDSEDLMH QKNEYITKKQ LFNATSIYLE AIYSLCVEG