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Protein

Peptidase E

Gene

pepE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.

Catalytic activityi

Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei120Charge relay system1 Publication1
Active sitei135Charge relay system1 Publication1
Active sitei157Charge relay system1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS51.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidase E (EC:3.4.13.21)
Alternative name(s):
Alpha-aspartyl dipeptidase
Asp-specific dipeptidase
Dipeptidase E
Gene namesi
Name:pepE
Ordered Locus Names:STM4190
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_00002099611 – 229Peptidase EAdd BLAST229

Proteomic databases

PaxDbiP36936.
PRIDEiP36936.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4190.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Turni16 – 20Combined sources5
Helixi21 – 28Combined sources8
Beta strandi33 – 37Combined sources5
Helixi46 – 57Combined sources12
Helixi58 – 60Combined sources3
Beta strandi63 – 66Combined sources4
Beta strandi69 – 71Combined sources3
Helixi73 – 79Combined sources7
Beta strandi81 – 85Combined sources5
Helixi90 – 99Combined sources10
Helixi103 – 111Combined sources9
Beta strandi115 – 119Combined sources5
Helixi121 – 125Combined sources5
Beta strandi127 – 130Combined sources4
Beta strandi150 – 155Combined sources6
Helixi171 – 181Combined sources11
Beta strandi186 – 189Combined sources4
Beta strandi195 – 198Combined sources4
Beta strandi203 – 209Combined sources7
Beta strandi211 – 215Combined sources5
Beta strandi218 – 223Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FY2X-ray1.20A1-229[»]
1FYEX-ray1.20A1-229[»]
ProteinModelPortaliP36936.
SMRiP36936.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36936.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S51 family.Curated

Phylogenomic databases

eggNOGiENOG4105EQ6. Bacteria.
COG3340. LUCA.
HOGENOMiHOG000281834.
KOiK05995.
OMAiKYTATVR.
PhylomeDBiP36936.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00510. Peptidase_E. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR005320. Peptidase_S51.
IPR023172. Peptidase_S51_dipeptidase-E.
[Graphical view]
PfamiPF03575. Peptidase_S51. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.

Sequencei

Sequence statusi: Complete.

P36936-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLLLSNST LPGKAWLEHA LPLIANQLNG RRSAVFIPFA GVTQTWDEYT
60 70 80 90 100
DKTAEVLAPL GVNVTGIHRV ADPLAAIEKA EIIIVGGGNT FQLLKESRER
110 120 130 140 150
GLLAPMADRV KRGALYIGWS AGANLACPTI RTTNDMPIVD PNGFDALDLF
160 170 180 190 200
PLQINPHFTN ALPEGHKGET REQRIRELLV VAPELTVIGL PEGNWIQVSN
210 220
GQAVLGGPNT TWVFKAGEEA VALEAGHRF
Length:229
Mass (Da):24,769
Last modified:June 1, 1994 - v1
Checksum:i41D40652C7D32220
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti120S → T in pepE1; deficient. 1
Natural varianti137P → S in pepE1; deficient. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01246 Unassigned DNA. Translation: AAA18923.1.
AE006468 Genomic DNA. Translation: AAL23014.1.
PIRiA36867.
RefSeqiNP_463055.1. NC_003197.1.
WP_000421792.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL23014; AAL23014; STM4190.
GeneIDi1255716.
KEGGistm:STM4190.
PATRICi32387273. VBISalEnt20916_4404.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01246 Unassigned DNA. Translation: AAA18923.1.
AE006468 Genomic DNA. Translation: AAL23014.1.
PIRiA36867.
RefSeqiNP_463055.1. NC_003197.1.
WP_000421792.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FY2X-ray1.20A1-229[»]
1FYEX-ray1.20A1-229[»]
ProteinModelPortaliP36936.
SMRiP36936.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM4190.

Protein family/group databases

MEROPSiS51.001.

Proteomic databases

PaxDbiP36936.
PRIDEiP36936.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL23014; AAL23014; STM4190.
GeneIDi1255716.
KEGGistm:STM4190.
PATRICi32387273. VBISalEnt20916_4404.

Phylogenomic databases

eggNOGiENOG4105EQ6. Bacteria.
COG3340. LUCA.
HOGENOMiHOG000281834.
KOiK05995.
OMAiKYTATVR.
PhylomeDBiP36936.

Miscellaneous databases

EvolutionaryTraceiP36936.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00510. Peptidase_E. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR005320. Peptidase_S51.
IPR023172. Peptidase_S51_dipeptidase-E.
[Graphical view]
PfamiPF03575. Peptidase_S51. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPEPE_SALTY
AccessioniPrimary (citable) accession number: P36936
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 110 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.