ID PEPT_ENTFA Reviewed; 409 AA.
AC Q835J5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 73.
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; Synonyms=pepT-1; OrderedLocusNames=EF_1382;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant
RT Enterococcus faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO81173.1; -; Genomic_DNA.
DR RefSeq; NP_815103.1; NC_004668.1.
DR ProteinModelPortal; Q835J5; -.
DR SMR; Q835J5; 3-409.
DR STRING; 226185.EF1382; -.
DR MEROPS; M20.003; -.
DR EnsemblBacteria; AAO81173; AAO81173; EF_1382.
DR GeneID; 1200282; -.
DR KEGG; efa:EF1382; -.
DR PATRIC; 21853140; VBIEntFae7065_1298.
DR eggNOG; COG2195; -.
DR KO; K01258; -.
DR OMA; YVYATIP; -.
DR ProtClustDB; PRK05469; -.
DR BioCyc; EFAE226185:GHI1-1470-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; Reference proteome; Zinc.
FT CHAIN 1 409 Peptidase T.
FT /FTId=PRO_0000185290.
FT ACT_SITE 82 82 By similarity.
FT ACT_SITE 177 177 Proton acceptor (By similarity).
FT METAL 80 80 Zinc 1 (By similarity).
FT METAL 143 143 Zinc 1 (By similarity).
FT METAL 143 143 Zinc 2 (By similarity).
FT METAL 178 178 Zinc 2 (By similarity).
FT METAL 200 200 Zinc 1 (By similarity).
FT METAL 382 382 Zinc 2 (By similarity).
SQ SEQUENCE 409 AA; 45400 MW; 445297A0CA825095 CRC64;
MYENLLPRFL RYVKTETRSD ATSTTTPSTQ TQVAFAQTLK KELEELGMSD VIYNETNGFV
IATLPSNVEK DVRSIGFIAH MDTADFNAVN VSPQIVENYD GESTIPLDKE GKFTLNTKDF
PNLKNYRGET LITTDGTTLL GADDKSGIAE IMTAMEYLIN HPEIKHGTIR VAFGPDEEIG
VGADKFDVAQ FNVDFAYTMD GGPVGELQFE TFNAAQAEIT IQGKNVHPGT AKNTMINALQ
LGIDFHNALP ADEVPEKTAG EEGFYHLAAF AGTPEEATMT YIIRDHNREI FEARKAKIKE
IQQTLNAPFD EERIKVDLFD QYYNMREVIE KDMSIVEIAK QAMEELSIQP IIEPVRGGTD
GSKISYLGIP TPNIFAGGEN MHGRFEFVSL QAMEKATNVI IKIAELNAK
//
