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P36936

- PEPE_SALTY

UniProt

P36936 - PEPE_SALTY

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
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    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

    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

    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: October 1, 2014
    This is version 98 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