Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P36936

- PEPE_SALTY

UniProt

P36936 - PEPE_SALTY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Peptidase E

Gene

pepE

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.

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)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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Peptidase EPRO_0000209961Add
BLAST

Proteomic databases

PRIDEiP36936.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4190.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Turni16 – 205Combined sources
Helixi21 – 288Combined sources
Beta strandi33 – 375Combined sources
Helixi46 – 5712Combined sources
Helixi58 – 603Combined sources
Beta strandi63 – 664Combined sources
Beta strandi69 – 713Combined sources
Helixi73 – 797Combined sources
Beta strandi81 – 855Combined sources
Helixi90 – 9910Combined sources
Helixi103 – 1119Combined sources
Beta strandi115 – 1195Combined sources
Helixi121 – 1255Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi150 – 1556Combined sources
Helixi171 – 18111Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi203 – 2097Combined sources
Beta strandi211 – 2155Combined sources
Beta strandi218 – 2236Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP36936.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S51 family.Curated

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

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

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.

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 .
PIRi A36867.
RefSeqi NP_463055.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 100 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