PEPT_ECOLI
ID PEPT_ECOLI Reviewed; 408 AA.
AC P29745; P77794;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
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=b1127, JW1113;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RC STRAIN=K12;
RX PubMed=1939142; DOI=10.1016/s0021-9258(18)54799-2;
RA Furuchi T., Kashiwagi K., Kobayashi H., Igarashi K.;
RT "Characteristics of the gene for a spermidine and putrescine transport
RT system that maps at 15 min on the Escherichia coli chromosome.";
RL J. Biol. Chem. 266:20928-20933(1991).
RN [5]
RP IDENTIFICATION.
RX PubMed=8244951; DOI=10.1128/jb.175.23.7745-7746.1993;
RA Lombardo M.-J., Miller C.G., Rudd K.E.;
RT "Physical mapping of the Escherichia coli pepT and potABCD genes.";
RL J. Bacteriol. 175:7745-7746(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-408 IN COMPLEX WITH ZINC,
RP COFACTOR, AND SUBUNIT.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16021622};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16021622};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:16021622}.
CC -!- INTERACTION:
CC P29745; P0A7C6: pepE; NbExp=4; IntAct=EBI-555639, EBI-555623;
CC P29745; P0A858: tpiA; NbExp=7; IntAct=EBI-555639, EBI-368978;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000305}.
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DR EMBL; U00096; AAC74211.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35949.1; -; Genomic_DNA.
DR EMBL; M64519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D64857; D64857.
DR RefSeq; NP_415645.1; NC_000913.3.
DR RefSeq; WP_000359434.1; NZ_SSZK01000010.1.
DR PDB; 1VIX; X-ray; 2.50 A; A/B=2-408.
DR PDBsum; 1VIX; -.
DR AlphaFoldDB; P29745; -.
DR SMR; P29745; -.
DR BioGRID; 4261675; 73.
DR BioGRID; 850690; 3.
DR DIP; DIP-10461N; -.
DR IntAct; P29745; 20.
DR STRING; 511145.b1127; -.
DR MEROPS; M20.003; -.
DR jPOST; P29745; -.
DR PaxDb; P29745; -.
DR PRIDE; P29745; -.
DR EnsemblBacteria; AAC74211; AAC74211; b1127.
DR EnsemblBacteria; BAA35949; BAA35949; BAA35949.
DR GeneID; 946333; -.
DR KEGG; ecj:JW1113; -.
DR KEGG; eco:b1127; -.
DR PATRIC; fig|1411691.4.peg.1139; -.
DR EchoBASE; EB1511; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_6; -.
DR InParanoid; P29745; -.
DR OMA; GHNFHGK; -.
DR PhylomeDB; P29745; -.
DR BioCyc; EcoCyc:EG11549-MON; -.
DR BioCyc; MetaCyc:EG11549-MON; -.
DR EvolutionaryTrace; P29745; -.
DR PRO; PR:P29745; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IDA:EcoCyc.
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:0006518; P:peptide metabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..408
FT /note="Peptidase T"
FT /id="PRO_0000185292"
FT ACT_SITE 80
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16021622"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16021622"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16021622"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16021622"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16021622"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16021622"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 139..157
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 260..283
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:1VIX"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:1VIX"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1VIX"
FT HELIX 387..406
FT /evidence="ECO:0007829|PDB:1VIX"
SQ SEQUENCE 408 AA; 44923 MW; 35751A1DF4CE6DA2 CRC64;
MDKLLERFLN YVSLDTQSKA GVRQVPSTEG QWKLLHLLKE QLEEMGLINV TLSEKGTLMA
TLPANVPGDI PAIGFISHVD TSPDCSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL
HQLLGQTLIT TDGKTLLGAD DKAGIAEIMT ALAVLQQKKI 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
