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Protein

Peptidase T

Gene

pepT

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N-blocked or C-blocked tripeptides, and tetrapeptides.1 Publication

Catalytic activityi

Release of the N-terminal residue from a tripeptide.

Cofactori

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

Enzyme regulationi

Inhibited by EDTA.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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1236-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:STM1227
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Peptidase TPRO_0000185312Add
BLAST

Proteomic databases

PaxDbiP26311.
PRIDEiP26311.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM1227.

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 129Combined sources
Beta strandi23 – 286Combined sources
Helixi29 – 4517Combined sources
Beta strandi48 – 525Combined sources
Beta strandi58 – 625Combined sources
Beta strandi73 – 786Combined sources
Beta strandi93 – 953Combined sources
Beta strandi106 – 1094Combined sources
Turni114 – 1163Combined sources
Helixi118 – 1225Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi133 – 1353Combined sources
Helixi139 – 15618Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi165 – 1717Combined sources
Helixi173 – 1753Combined sources
Turni178 – 1814Combined sources
Helixi184 – 1874Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi209 – 21810Combined sources
Helixi224 – 2263Combined sources
Turni228 – 2303Combined sources
Helixi234 – 24310Combined sources
Helixi251 – 2533Combined sources
Beta strandi260 – 2689Combined sources
Beta strandi270 – 28314Combined sources
Helixi284 – 30118Combined sources
Turni302 – 3043Combined sources
Beta strandi311 – 3199Combined 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
1FNOX-ray2.40A1-409[»]
ProteinModelPortaliP26311.
SMRiP26311. Positions 1-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26311.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 207207Catalytic N-terminalAdd
BLAST
Regioni208 – 318111DimerizationAdd
BLAST
Regioni319 – 40991Catalytic C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M20B family.Curated

Phylogenomic databases

eggNOGiENOG4105D42. Bacteria.
COG2195. LUCA.
HOGENOMiHOG000032390.
KOiK01258.
OMAiYVYATIP.
OrthoDBiEOG6SV59Q.
PhylomeDBiP26311.

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.

P26311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKLLERFLH YVSLDTQSKS GVRQVPSTEG QWKLLRLLKQ QLEEMGLVNI
60 70 80 90 100
TLSEKGTLMA TLPANVEGDI PAIGFISHVD TSPDFSGKNV NPQIVENYRG
110 120 130 140 150
GDIALGIGDE VLSPVMFPVL HQLLGQTLIT TDGKTLLGAD DKAGVAEIMT
160 170 180 190 200
ALAVLKGNPI PHGDIKVAFT PDEEVGKGAK HFDVEAFGAQ WAYTVDGGGV
210 220 230 240 250
GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR IHAEVPADEA
260 270 280 290 300
PETTEGYEGF YHLASMKGTV DRAEMHYIIR DFDRKQFEAR KRKMMEIAKK
310 320 330 340 350
VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCHITPEMK
360 370 380 390 400
PIRGGTDGAQ LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI

AELTAKRGQ
Length:409
Mass (Da):44,849
Last modified:May 1, 1992 - v1
Checksum:i7943CBFAD74017A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62725 Genomic DNA. Translation: AAA27183.1.
AE006468 Genomic DNA. Translation: AAL20156.1.
PIRiA42363.
RefSeqiNP_460197.1. NC_003197.1.
WP_000359410.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20156; AAL20156; STM1227.
GeneIDi1252745.
KEGGistm:STM1227.
PATRICi32380907. VBISalEnt20916_1298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62725 Genomic DNA. Translation: AAA27183.1.
AE006468 Genomic DNA. Translation: AAL20156.1.
PIRiA42363.
RefSeqiNP_460197.1. NC_003197.1.
WP_000359410.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNOX-ray2.40A1-409[»]
ProteinModelPortaliP26311.
SMRiP26311. Positions 1-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1227.

Protein family/group databases

MEROPSiM20.003.

Proteomic databases

PaxDbiP26311.
PRIDEiP26311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20156; AAL20156; STM1227.
GeneIDi1252745.
KEGGistm:STM1227.
PATRICi32380907. VBISalEnt20916_1298.

Phylogenomic databases

eggNOGiENOG4105D42. Bacteria.
COG2195. LUCA.
HOGENOMiHOG000032390.
KOiK01258.
OMAiYVYATIP.
OrthoDBiEOG6SV59Q.
PhylomeDBiP26311.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1236-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP26311.

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. "Cloning and nucleotide sequence of the anaerobically regulated pepT gene of Salmonella typhimurium."
    Miller C.G., Miller J.L., Bagga D.A.
    J. Bacteriol. 173:3554-3558(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Isolation and characterization Salmonella typhimurium mutants lacking a tripeptidase (peptidase T)."
    Strauch K.L., Miller C.G.
    J. Bacteriol. 154:763-771(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
  4. "Crystallization of peptidase T from Salmonella typhimurium."
    Hakansson K., Broder D., Wang A.H., Miller C.G.
    Acta Crystallogr. D 56:924-926(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  5. "Structure of peptidase T from Salmonella typhimurium."
    Hakansson K., Miller C.G.
    Eur. J. Biochem. 269:443-450(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPEPT_SALTY
AccessioniPrimary (citable) accession number: P26311
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 11, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.