Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P36936 (PEPE_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidase E

EC=3.4.13.21
Alternative name(s):
Alpha-aspartyl dipeptidase
Asp-specific dipeptidase
Dipeptidase E
Gene names
Name:pepE
Ordered Locus Names:STM4190
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00510

Catalytic activity

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. HAMAP-Rule MF_00510

Subcellular location

Cytoplasm HAMAP-Rule MF_00510.

Sequence similarities

Belongs to the peptidase S51 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionDipeptidase
Hydrolase
Protease
Serine protease
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondipeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Peptidase E HAMAP-Rule MF_00510
PRO_0000209961

Sites

Active site1201Charge relay system Ref.3
Active site1351Charge relay system Ref.3
Active site1571Charge relay system Ref.3

Natural variations

Natural variant1201S → T in pepE1; deficient.
Natural variant1371P → S in pepE1; deficient.

Secondary structure

........................................... 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36936 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 41D40652C7D32220

FASTA22924,769
        10         20         30         40         50         60 
MELLLLSNST LPGKAWLEHA LPLIANQLNG RRSAVFIPFA GVTQTWDEYT DKTAEVLAPL 

        70         80         90        100        110        120 
GVNVTGIHRV ADPLAAIEKA EIIIVGGGNT FQLLKESRER GLLAPMADRV KRGALYIGWS 

       130        140        150        160        170        180 
AGANLACPTI RTTNDMPIVD PNGFDALDLF PLQINPHFTN ALPEGHKGET REQRIRELLV 

       190        200        210        220 
VAPELTVIGL PEGNWIQVSN GQAVLGGPNT TWVFKAGEEA VALEAGHRF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an alpha-aspartyl dipeptidase."
Conlin C.A., Hakensson K., Liljas A., Miller C.G.
J. Bacteriol. 176:166-172(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25.
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase."
Lassy R.A., Miller C.G.
J. Bacteriol. 182:2536-2543(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, ACTIVE SITES, MUTAGENESIS.
[4]"The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad."
Hakansson K., Wang A.H.-J., Miller C.G.
Proc. Natl. Acad. Sci. U.S.A. 97:14097-14102(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01246 Unassigned DNA. Translation: AAA18923.1.
AE006468 Genomic DNA. Translation: AAL23014.1.
PIRA36867.
RefSeqNP_463055.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FY2X-ray1.20A1-229[»]
1FYEX-ray1.20A1-229[»]
ProteinModelPortalP36936.
SMRP36936. Positions 1-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM4190.

Protein family/group databases

MEROPSS51.001.

Proteomic databases

PRIDEP36936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL23014; AAL23014; STM4190.
GeneID1255716.
KEGGstm:STM4190.
PATRIC32387273. VBISalEnt20916_4404.

Phylogenomic databases

HOGENOMHOG000281834.
KOK05995.
OMASEATANH.
OrthoDBEOG6M6JST.
PhylomeDBP36936.

Enzyme and pathway databases

BioCycSENT99287:GCTI-4220-MONOMER.

Family and domain databases

Gene3D3.40.50.880. 1 hit.
HAMAPMF_00510. Peptidase_E.
InterProIPR029062. Class_I_gatase-like.
IPR005320. Peptidase_S51.
IPR023172. Peptidase_S51_dipeptidase-E.
[Graphical view]
PfamPF03575. Peptidase_S51. 1 hit.
[Graphical view]
SUPFAMSSF52317. SSF52317. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP36936.

Entry information

Entry namePEPE_SALTY
AccessionPrimary (citable) accession number: P36936
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references