ID   PEPVL_STAAW             Reviewed;         469 AA.
AC   Q8NW23;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative dipeptidase MW1694;
DE            EC=3.4.13.-;
GN   OrderedLocusNames=MW1694;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95559.1; -; Genomic_DNA.
DR   RefSeq; WP_000265409.1; NC_003923.1.
DR   AlphaFoldDB; Q8NW23; -.
DR   SMR; Q8NW23; -.
DR   EnsemblBacteria; BAB95559; BAB95559; BAB95559.
DR   KEGG; sam:MW1694; -.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   OMA; GYAGHIE; -.
DR   Proteomes; UP000000418; 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 MW1694"
FT                   /id="PRO_0000282633"
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;  52808 MW;  DC2046B8565B8FAB CRC64;
     MWKEKVQQYE DQIINDLKGL LAIESVRDDA KASEDAPVGP GPRKALDYMY EIAHRDGFTT
     HDVDHIAGRI EAGKGNDVLG ILCHVDVVPA GDGWDSNPFE PVVTEDAIIA RGTLDDKGPT
     IAAYYAIKIL EDMNVDWKKR IHMIIGTDEE SDWKCTDRYF KTEEMPTLGF APDAEFPCIH
     GEKGITTFDL VQNKLAEDQD EPDYELITFK SGERYNMVPD HAEARVLVKE NMTDVIQDFE
     YFLEQNHLQG DSTVDSGILV LTVEGKAVHG MDPSIGVNAG LYLLKFLASL NLDNNAQAFV
     AFSNRYLFDS DFGEKMGMKF HTDVMGDVTN NIGVITYDNE NAGLFGINLR YPEGFEFEKA
     MDRFANEIQQ YGFEVKLGKV QPPHYVDKND PFVQKLVTAY RNQTNDMTEP YTIGGGTYAR
     NLDKGVAFGA MFSDSEDLMH QKNEYITKKQ LFNATSIYLE AIYSLCVEE