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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)DescriptionActionsGraphical viewLength
Metal bindingi78Zinc 11 Publication1
Active sitei80By similarity1
Metal bindingi140Zinc 11 Publication1
Metal bindingi140Zinc 21 Publication1
Active sitei173Proton acceptorBy similarity1
Metal bindingi174Zinc 21 Publication1
Metal bindingi196Zinc 11 Publication1
Metal bindingi379Zinc 21 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001853121 – 409Peptidase TAdd BLAST409

Proteomic databases

PaxDbiP26311.
PRIDEiP26311.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM1227.

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 12Combined sources9
Beta strandi23 – 28Combined sources6
Helixi29 – 45Combined sources17
Beta strandi48 – 52Combined sources5
Beta strandi58 – 62Combined sources5
Beta strandi73 – 78Combined sources6
Beta strandi93 – 95Combined sources3
Beta strandi106 – 109Combined sources4
Turni114 – 116Combined sources3
Helixi118 – 122Combined sources5
Beta strandi128 – 130Combined sources3
Beta strandi133 – 135Combined sources3
Helixi139 – 156Combined sources18
Beta strandi157 – 159Combined sources3
Beta strandi165 – 171Combined sources7
Helixi173 – 175Combined sources3
Turni178 – 181Combined sources4
Helixi184 – 187Combined sources4
Beta strandi190 – 194Combined sources5
Beta strandi202 – 204Combined sources3
Beta strandi209 – 218Combined sources10
Helixi224 – 226Combined sources3
Turni228 – 230Combined sources3
Helixi234 – 243Combined sources10
Helixi251 – 253Combined sources3
Beta strandi260 – 268Combined sources9
Beta strandi270 – 283Combined sources14
Helixi284 – 301Combined sources18
Turni302 – 304Combined sources3
Beta strandi311 – 319Combined sources9
Helixi323 – 327Combined sources5
Helixi331 – 342Combined sources12
Beta strandi352 – 354Combined sources3
Helixi357 – 361Combined sources5
Turni362 – 365Combined sources4
Beta strandi374 – 377Combined sources4
Beta strandi384 – 386Combined sources3
Helixi387 – 406Combined sources20

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26311.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 207Catalytic N-terminalAdd BLAST207
Regioni208 – 318DimerizationAdd BLAST111
Regioni319 – 409Catalytic C-terminalAdd BLAST91

Sequence similaritiesi

Belongs to the peptidase M20B family.Curated

Phylogenomic databases

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

Family and domain databases

CDDicd03892. M20_peptT. 1 hit.
Gene3Di3.30.70.360. 1 hit.
HAMAPiMF_00550. Aminopeptidase_M20. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNOX-ray2.40A1-409[»]
ProteinModelPortaliP26311.
SMRiP26311.
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.
PhylomeDBiP26311.

Miscellaneous databases

EvolutionaryTraceiP26311.

Family and domain databases

CDDicd03892. M20_peptT. 1 hit.
Gene3Di3.30.70.360. 1 hit.
HAMAPiMF_00550. Aminopeptidase_M20. 1 hit.
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...

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 2, 2016
This is version 123 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.