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-MAY-2013, entry version 40.
DE RecName: Full=Peptidase T;
DE EC=3.4.11.4;
DE AltName: Full=Aminotripeptidase;
DE Short=Tripeptidase;
DE AltName: Full=Tripeptide aminopeptidase;
GN Name=pepT; 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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Release of the N-terminal residue from a
CC tripeptide.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M20B family.
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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 GeneID; 6947877; -.
DR KEGG; set:SEN1822; -.
DR PATRIC; 32334145; VBISalEnt14964_1853.
DR eggNOG; COG2195; -.
DR HOGENOM; HOG000032390; -.
DR KO; K01258; -.
DR OMA; YVYATIP; -.
DR ProtClustDB; PRK05469; -.
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:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:HAMAP.
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; Peptidase_M20_dimer; 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 By similarity.
FT ACT_SITE 173 173 Proton acceptor (By similarity).
FT METAL 78 78 Zinc 1 (By similarity).
FT METAL 140 140 Zinc 1 (By similarity).
FT METAL 140 140 Zinc 2 (By similarity).
FT METAL 174 174 Zinc 2 (By similarity).
FT METAL 196 196 Zinc 1 (By similarity).
FT METAL 379 379 Zinc 2 (By similarity).
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
//
