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Database: UniProt
Entry: Q835J5
LinkDB: Q835J5
Original site: Q835J5 
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   29-OCT-2014, entry version 80.
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}; Synonyms=pepT-1;
GN   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.
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; 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; HENYDGE; -.
DR   OrthoDB; EOG6SV59Q; -.
DR   BioCyc; EFAE226185:GHI1-1369-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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; Reference proteome; Zinc.
FT   CHAIN         1    409       Peptidase T.
FT                                /FTId=PRO_0000185290.
FT   ACT_SITE     82     82       {ECO:0000255|HAMAP-Rule:MF_00550}.
FT   ACT_SITE    177    177       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL        80     80       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       143    143       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       143    143       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       178    178       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       200    200       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
FT   METAL       382    382       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00550}.
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
//
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