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Database: UniProt
Entry: B5QXA9
LinkDB: B5QXA9
Original site: B5QXA9 
ID   PEPT_SALEP              Reviewed;         409 AA.
AC   B5QXA9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   01-OCT-2014, entry version 47.
DE   RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550};
DE            EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550};
DE   AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE            Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
DE   AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550};
GN   Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550};
GN   OrderedLocusNames=SEN1822;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K.,
RA   Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A.,
RA   Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G.,
RA   Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and
RT   Salmonella gallinarum 287/91 provides insights into evolutionary and
RT   host adaptation pathways.";
RL   Genome Res. 18:1624-1637(2008).
CC   -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC       {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- CATALYTIC ACTIVITY: Release of the N-terminal residue from a
CC       tripeptide. {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00550}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- SIMILARITY: Belongs to the peptidase M20B family.
CC       {ECO:0000255|HAMAP-Rule:MF_00550}.
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DR   EMBL; AM933172; CAR33402.1; -; Genomic_DNA.
DR   RefSeq; YP_002243917.1; NC_011294.1.
DR   ProteinModelPortal; B5QXA9; -.
DR   STRING; 550537.SEN1822; -.
DR   MEROPS; M20.003; -.
DR   EnsemblBacteria; CAR33402; CAR33402; SEN1822.
DR   PATRIC; 32334145; VBISalEnt14964_1853.
DR   eggNOG; COG2195; -.
DR   HOGENOM; HOG000032390; -.
DR   OMA; DCYIEVT; -.
DR   OrthoDB; EOG6SV59Q; -.
DR   BioCyc; SENT550537:GJFI-1840-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   HAMAP; MF_00550; Aminopeptidase_M20; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010161; Peptidase_M20B.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01882; peptidase-T; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN         1    409       Peptidase T.
FT                                /FTId=PRO_1000129040.
FT   ACT_SITE     80     80       {ECO:0000255|HAMAP-Rule:MF_00550}.
FT   ACT_SITE    173    173       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL        78     78       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       140    140       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       140    140       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       174    174       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       196    196       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       379    379       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
SQ   SEQUENCE   409 AA;  44893 MW;  FE85AC21A75DD667 CRC64;
     MDKLLERFLH YVSLDTQSKS GVRQVPSTEG QWKLLRLLKQ QLEEMGLVNI TLSEKGTLMA
     TLPANVEGDI PAIGFISHVD TSPDFSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL
     HQLLGQTLIT TDGKTLLGAD DKAGVAEIMT ALAVLKGNPI PHGEIKVAFT PDEEVGKGAK
     HFDVEAFGAQ WAYTVDGGGV GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR
     IHAEVPADET PETTEGYEGF YHLASMKGTV DRAEMHYIIR DFDRKQFEAR KRKMMEIAKK
     VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCHITPEMK PIRGGTDGAQ
     LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI AELTAKRGQ
//
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