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Protein

Peptidase T

Gene

pepT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the N-terminal amino acid of tripeptides.By similarity

Catalytic activityi

Release of the N-terminal residue from a tripeptide.

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi78 – 781Zinc 11 Publication
Active sitei80 – 801By similarity
Metal bindingi140 – 1401Zinc 11 Publication
Metal bindingi140 – 1401Zinc 21 Publication
Active sitei173 – 1731Proton acceptorBy similarity
Metal bindingi174 – 1741Zinc 21 Publication
Metal bindingi196 – 1961Zinc 11 Publication
Metal bindingi379 – 3791Zinc 21 Publication

GO - Molecular functioni

  • metallopeptidase activity Source: UniProtKB-KW
  • tripeptide aminopeptidase activity Source: EcoCyc
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • peptide catabolic process Source: UniProtKB-HAMAP
  • peptide metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG11549-MONOMER.
ECOL316407:JW1113-MONOMER.
MetaCyc:EG11549-MONOMER.

Protein family/group databases

MEROPSiM20.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidase T (EC:3.4.11.4)
Alternative name(s):
Aminotripeptidase
Short name:
Tripeptidase
Tripeptide aminopeptidase
Gene namesi
Name:pepT
Ordered Locus Names:b1127, JW1113
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11549. pepT.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408Peptidase TPRO_0000185292Add
BLAST

Proteomic databases

PaxDbiP29745.
PRIDEiP29745.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
tpiAP0A8584EBI-555639,EBI-368978

Protein-protein interaction databases

BioGridi4261675. 14 interactions.
DIPiDIP-10461N.
IntActiP29745. 19 interactions.
MINTiMINT-1219063.
STRINGi511145.b1127.

Structurei

Secondary structure

1
408
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Beta strandi23 – 286Combined sources
Helixi30 – 4314Combined sources
Turni44 – 463Combined sources
Beta strandi48 – 525Combined sources
Beta strandi58 – 625Combined sources
Beta strandi73 – 786Combined sources
Beta strandi93 – 953Combined sources
Beta strandi103 – 1053Combined sources
Turni106 – 1094Combined sources
Beta strandi110 – 1123Combined sources
Turni114 – 1163Combined sources
Helixi118 – 1225Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi133 – 1353Combined sources
Helixi139 – 15719Combined sources
Beta strandi165 – 1717Combined sources
Helixi173 – 1753Combined sources
Turni178 – 1814Combined sources
Helixi184 – 1874Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi209 – 21810Combined sources
Helixi224 – 2263Combined sources
Turni228 – 2303Combined sources
Helixi234 – 24411Combined sources
Turni251 – 2533Combined sources
Beta strandi260 – 28324Combined sources
Helixi284 – 30219Combined sources
Beta strandi310 – 31910Combined sources
Helixi323 – 3275Combined sources
Helixi331 – 34212Combined sources
Beta strandi352 – 3543Combined sources
Helixi357 – 3615Combined sources
Turni362 – 3654Combined sources
Beta strandi374 – 3774Combined sources
Beta strandi384 – 3863Combined sources
Helixi387 – 40620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VIXX-ray2.50A/B2-408[»]
ProteinModelPortaliP29745.
SMRiP29745. Positions 1-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29745.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20B family.Curated

Phylogenomic databases

eggNOGiENOG4105D42. Bacteria.
COG2195. LUCA.
HOGENOMiHOG000032390.
InParanoidiP29745.
KOiK01258.
OMAiYVYATIP.
OrthoDBiEOG6SV59Q.
PhylomeDBiP29745.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
HAMAPiMF_00550. Aminopeptidase_M20.
InterProiIPR001261. ArgE/DapE_CS.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
IPR010161. Peptidase_M20B.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037215. Peptidase_M20B. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01882. peptidase-T. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKLLERFLN YVSLDTQSKA GVRQVPSTEG QWKLLHLLKE QLEEMGLINV
60 70 80 90 100
TLSEKGTLMA TLPANVPGDI PAIGFISHVD TSPDCSGKNV NPQIVENYRG
110 120 130 140 150
GDIALGIGDE VLSPVMFPVL HQLLGQTLIT TDGKTLLGAD DKAGIAEIMT
160 170 180 190 200
ALAVLQQKKI PHGDIRVAFT PDEEVGKGAK HFDVDAFDAR WAYTVDGGGV
210 220 230 240 250
GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR IHAEVPADES
260 270 280 290 300
PEMTEGYEGF YHLASMKGTV ERADMHYIIR DFDRKQFEAR KRKMMEIAKK
310 320 330 340 350
VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCDIEPELK
360 370 380 390 400
PIRGGTDGAQ LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI

AELTAQRK
Length:408
Mass (Da):44,923
Last modified:November 1, 1997 - v2
Checksum:i35751A1DF4CE6DA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74211.1.
AP009048 Genomic DNA. Translation: BAA35949.1.
M64519 Genomic DNA. No translation available.
PIRiD64857.
RefSeqiNP_415645.1. NC_000913.3.
WP_000359434.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74211; AAC74211; b1127.
BAA35949; BAA35949; BAA35949.
GeneIDi946333.
KEGGiecj:JW1113.
eco:b1127.
PATRICi32117503. VBIEscCol129921_1174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74211.1.
AP009048 Genomic DNA. Translation: BAA35949.1.
M64519 Genomic DNA. No translation available.
PIRiD64857.
RefSeqiNP_415645.1. NC_000913.3.
WP_000359434.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VIXX-ray2.50A/B2-408[»]
ProteinModelPortaliP29745.
SMRiP29745. Positions 1-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261675. 14 interactions.
DIPiDIP-10461N.
IntActiP29745. 19 interactions.
MINTiMINT-1219063.
STRINGi511145.b1127.

Protein family/group databases

MEROPSiM20.003.

Proteomic databases

PaxDbiP29745.
PRIDEiP29745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74211; AAC74211; b1127.
BAA35949; BAA35949; BAA35949.
GeneIDi946333.
KEGGiecj:JW1113.
eco:b1127.
PATRICi32117503. VBIEscCol129921_1174.

Organism-specific databases

EchoBASEiEB1511.
EcoGeneiEG11549. pepT.

Phylogenomic databases

eggNOGiENOG4105D42. Bacteria.
COG2195. LUCA.
HOGENOMiHOG000032390.
InParanoidiP29745.
KOiK01258.
OMAiYVYATIP.
OrthoDBiEOG6SV59Q.
PhylomeDBiP29745.

Enzyme and pathway databases

BioCyciEcoCyc:EG11549-MONOMER.
ECOL316407:JW1113-MONOMER.
MetaCyc:EG11549-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP29745.
PROiP29745.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
HAMAPiMF_00550. Aminopeptidase_M20.
InterProiIPR001261. ArgE/DapE_CS.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
IPR010161. Peptidase_M20B.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037215. Peptidase_M20B. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01882. peptidase-T. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome."
    Furuchi T., Kashiwagi K., Kobayashi H., Igarashi K.
    J. Biol. Chem. 266:20928-20933(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
    Strain: K12.
  5. "Physical mapping of the Escherichia coli pepT and potABCD genes."
    Lombardo M.-J., Miller C.G., Rudd K.E.
    J. Bacteriol. 175:7745-7746(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-408 IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPEPT_ECOLI
AccessioniPrimary (citable) accession number: P29745
Secondary accession number(s): P77794
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.