ID   PEPT_ECOUT              Reviewed;         408 AA.
AC   Q1RD26;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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}; OrderedLocusNames=UTI89_C1256;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC       {ECO:0000255|HAMAP-Rule:MF_00550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of the N-terminal residue from a tripeptide.;
CC         EC=3.4.11.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00550};
CC       Note=Binds 2 Zn(2+) 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. {ECO:0000255|HAMAP-
CC       Rule:MF_00550}.
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DR   EMBL; CP000243; ABE06738.1; -; Genomic_DNA.
DR   RefSeq; WP_000359446.1; NC_007946.1.
DR   AlphaFoldDB; Q1RD26; -.
DR   SMR; Q1RD26; -.
DR   MEROPS; M20.003; -.
DR   EnsemblBacteria; ABE06738; ABE06738; UTI89_C1256.
DR   GeneID; 58461245; -.
DR   KEGG; eci:UTI89_C1256; -.
DR   HOGENOM; CLU_053676_0_0_6; -.
DR   OMA; GHNFHGK; -.
DR   Proteomes; UP000001952; Chromosome.
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-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00550; Aminopeptidase_M20; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010161; Peptidase_M20B.
DR   PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
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; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Zinc.
FT   CHAIN           1..408
FT                   /note="Peptidase T"
FT                   /id="PRO_0000274014"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
FT   BINDING         379
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00550"
SQ   SEQUENCE   408 AA;  44909 MW;  35744B1DF4CC1DA2 CRC64;
     MDKLLERFLN YVSLDTQSKA GVRQVPSTEG QWKLLHLLKE QLEEMGLINV TLSEKGTLMA
     TLPANVPGDI PAIGFISHVD TSPDCSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL
     HQLLGQTLIT TDGKTLLGAD DKAGIAEIMT ALAVLQQKNI PHGDIRVAFT PDEEVGKGAK
     HFDVDAFDAR WAYTVDGGGV GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR
     IHAEVPADES PEMTEGYEGF YHLASMKGTV ERADMHYIIR DFDRKQFEAR KRKMMEIAKK
     VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCDIEPELK PIRGGTDGAQ
     LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI AELTAQRK