PEPVL_STAS1
ID PEPVL_STAS1 Reviewed; 469 AA.
AC Q49YI2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative dipeptidase SSP1012;
DE EC=3.4.13.-;
GN OrderedLocusNames=SSP1012;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18157.1; -; Genomic_DNA.
DR RefSeq; WP_011302862.1; NZ_MTGA01000033.1.
DR AlphaFoldDB; Q49YI2; -.
DR SMR; Q49YI2; -.
DR STRING; 342451.SSP1012; -.
DR EnsemblBacteria; BAE18157; BAE18157; SSP1012.
DR KEGG; ssp:SSP1012; -.
DR PATRIC; fig|342451.11.peg.1011; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_031786_2_0_9; -.
DR OMA; GYAGHIE; -.
DR OrthoDB; 906744at2; -.
DR Proteomes; UP000006371; 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 SSP1012"
FT /id="PRO_0000282637"
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; 52699 MW; 6B7169E305904AEA CRC64;
MWRDKVKEYE DFILEDLKGL LSIESVREDD KASAENPVGP GPRQALDYMY KIAERDGFGT
HDVDHIAGRI EAGKGDDVFG ILCHVDVVPA GDGWDSDPFN PVVTDDKIIA RGTLDDKGPT
IAAYYAVKIL NEMNVNWKKR IHIIIGTDEE SDWKCTERYF QTEEMPELGF APDAEFPAIH
GEKGISTFDV IQNEKADDQD EPEYELRSFV SGQRYNMVPD EAIANVAVKE NMTDVIQNFE
QYLNEHDVEG ESVVDSGVLV LKVQGKAVHG MDPSIGVNAG LYLLNFLATL NLDKTAANFV
AFSERYLFES HFGEKMGMKF HTDVMGDVTT NVGIITYDNQ DGGKFGINLR YPEGFEFEES
LTRFKGEIQS LGFSIELGKN QTPHYVEKDD PFLQSLVQAY RNQTGDDTEP YTIGGGTYAR
NLDKGVAFGA MFSDSEDLMH QKNEYITKKQ LFNATSIYLE SLYKLCVEE