PEPVL_STAA8
ID PEPVL_STAA8 Reviewed; 469 AA.
AC Q2FXH9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Putative dipeptidase SAOUHSC_01868;
DE EC=3.4.13.-;
GN OrderedLocusNames=SAOUHSC_01868;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD30933.1; -; Genomic_DNA.
DR RefSeq; WP_000265417.1; NZ_LS483365.1.
DR RefSeq; YP_500371.1; NC_007795.1.
DR AlphaFoldDB; Q2FXH9; -.
DR SMR; Q2FXH9; -.
DR STRING; 1280.SAXN108_1782; -.
DR EnsemblBacteria; ABD30933; ABD30933; SAOUHSC_01868.
DR GeneID; 3921757; -.
DR KEGG; sao:SAOUHSC_01868; -.
DR PATRIC; fig|93061.5.peg.1700; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_031786_2_0_9; -.
DR OMA; GYAGHIE; -.
DR PRO; PR:Q2FXH9; -.
DR Proteomes; UP000008816; 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;
KW Reference proteome; Zinc.
FT CHAIN 1..469
FT /note="Putative dipeptidase SAOUHSC_01868"
FT /id="PRO_0000282627"
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