ID   PEPVL_STAAR             Reviewed;         469 AA.
AC   Q6GFV0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Putative dipeptidase SAR1836;
DE            EC=3.4.13.-;
GN   OrderedLocusNames=SAR1836;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40827.1; -; Genomic_DNA.
DR   RefSeq; WP_000265408.1; NC_002952.2.
DR   AlphaFoldDB; Q6GFV0; -.
DR   SMR; Q6GFV0; -.
DR   KEGG; sar:SAR1836; -.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   OMA; GYAGHIE; -.
DR   OrthoDB; 906744at2; -.
DR   Proteomes; UP000000596; 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   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
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 SAR1836"
FT                   /id="PRO_0000282631"
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;  52794 MW;  99E8A16E49512637 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 NLDNNAKAFV
     AFSNRYLFNS DFGEKMGMKF HTDVMGDVTT NIGVITYDNE NAGLFGINLR YPEGFEFEKA
     MDRFANEIQQ YGFEVKLGKV QPPHYVDKND PFVQKLVTAY RNQTNDMTEP YTIGGGTYAR
     NLDKGVAFGA MFSDSEDLMH QKNEYITKKQ LFNATSIYLE AIYSLCVEE