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P36936

- PEPE_SALTY

UniProt

P36936 - PEPE_SALTY

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Protein
Peptidase E
Gene
pepE, STM4190
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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.UniRule annotation

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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei120 – 1201Charge relay system1 Publication
Active sitei135 – 1351Charge relay system1 Publication
Active sitei157 – 1571Charge relay system1 Publication

GO - Molecular functioni

  1. dipeptidase activity Source: UniProtKB-HAMAP
  2. serine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BioCyciSENT99287:GCTI-4220-MONOMER.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Peptidase EUniRule annotation
PRO_0000209961Add
BLAST

Proteomic databases

PRIDEiP36936.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4190.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76
Turni16 – 205
Helixi21 – 288
Beta strandi33 – 375
Helixi46 – 5712
Helixi58 – 603
Beta strandi63 – 664
Beta strandi69 – 713
Helixi73 – 797
Beta strandi81 – 855
Helixi90 – 9910
Helixi103 – 1119
Beta strandi115 – 1195
Helixi121 – 1255
Beta strandi127 – 1304
Beta strandi150 – 1556
Helixi171 – 18111
Beta strandi186 – 1894
Beta strandi195 – 1984
Beta strandi203 – 2097
Beta strandi211 – 2155
Beta strandi218 – 2236

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FY2X-ray1.20A1-229[»]
1FYEX-ray1.20A1-229[»]
ProteinModelPortaliP36936.
SMRiP36936. Positions 1-229.

Miscellaneous databases

EvolutionaryTraceiP36936.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S51 family.

Phylogenomic databases

HOGENOMiHOG000281834.
KOiK05995.
OMAiSEATANH.
OrthoDBiEOG6M6JST.
PhylomeDBiP36936.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00510. Peptidase_E.
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

MELLLLSNST LPGKAWLEHA LPLIANQLNG RRSAVFIPFA GVTQTWDEYT    50
DKTAEVLAPL GVNVTGIHRV ADPLAAIEKA EIIIVGGGNT FQLLKESRER 100
GLLAPMADRV KRGALYIGWS AGANLACPTI RTTNDMPIVD PNGFDALDLF 150
PLQINPHFTN ALPEGHKGET REQRIRELLV VAPELTVIGL PEGNWIQVSN 200
GQAVLGGPNT TWVFKAGEEA VALEAGHRF 229
Length:229
Mass (Da):24,769
Last modified:June 1, 1994 - v1
Checksum:i41D40652C7D32220
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201S → T in pepE1; deficient.
Natural varianti137 – 1371P → S in pepE1; deficient.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01246 Unassigned DNA. Translation: AAA18923.1.
AE006468 Genomic DNA. Translation: AAL23014.1.
PIRiA36867.
RefSeqiNP_463055.1. NC_003197.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01246 Unassigned DNA. Translation: AAA18923.1 .
AE006468 Genomic DNA. Translation: AAL23014.1 .
PIRi A36867.
RefSeqi NP_463055.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FY2 X-ray 1.20 A 1-229 [» ]
1FYE X-ray 1.20 A 1-229 [» ]
ProteinModelPortali P36936.
SMRi P36936. Positions 1-229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM4190.

Protein family/group databases

MEROPSi S51.001.

Proteomic databases

PRIDEi P36936.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL23014 ; AAL23014 ; STM4190 .
GeneIDi 1255716.
KEGGi stm:STM4190.
PATRICi 32387273. VBISalEnt20916_4404.

Phylogenomic databases

HOGENOMi HOG000281834.
KOi K05995.
OMAi SEATANH.
OrthoDBi EOG6M6JST.
PhylomeDBi P36936.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-4220-MONOMER.

Miscellaneous databases

EvolutionaryTracei P36936.

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
HAMAPi MF_00510. Peptidase_E.
InterProi IPR029062. Class_I_gatase-like.
IPR005320. Peptidase_S51.
IPR023172. Peptidase_S51_dipeptidase-E.
[Graphical view ]
Pfami PF03575. Peptidase_S51. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

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: July 9, 2014
This is version 97 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

External Data

Dasty 3

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