ID   PEPVL_STAAM             Reviewed;         469 AA.
AC   Q7A2R1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Putative dipeptidase SAV1751;
DE            EC=3.4.13.-;
GN   OrderedLocusNames=SAV1751;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57913.1; -; Genomic_DNA.
DR   RefSeq; WP_000265417.1; NC_002758.2.
DR   AlphaFoldDB; Q7A2R1; -.
DR   SMR; Q7A2R1; -.
DR   World-2DPAGE; 0002:Q7A2R1; -.
DR   PaxDb; Q7A2R1; -.
DR   EnsemblBacteria; BAB57913; BAB57913; SAV1751.
DR   KEGG; sav:SAV1751; -.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   OMA; GYAGHIE; -.
DR   PhylomeDB; Q7A2R1; -.
DR   BioCyc; SAUR158878:SAV_RS09415-MON; -.
DR   Proteomes; UP000002481; 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 SAV1751"
FT                   /id="PRO_0000282629"
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;  52824 MW;  589267D3EEC82350 CRC64;
     MWKEKVQQYE DQIINDLKGL LAIESVRDDA KASEDAPVGP GPRKALDYMY EIAHRDGFTT
     HDVDHIAGRI EAGKGNDVLG ILCHVDVVPA GDGWDSNPFE PVVTEDAIIA RGTLDDKGPT
     IAAYYAIKIL EDMNVDWKKR IHMIIGTDEE SDWKCTDRYF KTEEMPTLGF APDAEFPCIH
     GEKGITTFDL VQNKLTEDQD EPDYELITFK SGERYNMVPD HAEARVLVKE NMTDVIQDFE
     YFLEQNHLQG DSTVDSGILV LTVEGKAVHG MDPSIGVNAG LYLLKFLASL NLDNNAQAFV
     AFSNRYLFNS DFGEKMGMKF HTDVMGDVTT NIGVITYDNE NAGLFGINLR YPEGFEFEKA
     MDRFANEIQQ YGFEVKLGKV QPPHYVDKND PFVQKLVTAY RNQTNDMTEP YTIGGGTYAR
     NLDKGVAFGA MFSDSEDLMH QKNEYITKKQ LFNATSIYLE AIYSLCVEE