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P09372

- GRPE_ECOLI

UniProt

P09372 - GRPE_ECOLI

Protein

Protein GrpE

Gene

grpE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei183 – 1831Interaction with DnaK

    GO - Molecular functioni

    1. adenyl-nucleotide exchange factor activity Source: InterPro

    GO - Biological processi

    1. protein folding Source: InterPro
    2. protein unfolding Source: EcoCyc
    3. response to heat Source: EcoliWiki

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10416-MONOMER.
    ECOL316407:JW2594-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein GrpE
    Alternative name(s):
    HSP-70 cofactor
    HSP24
    Heat shock protein B25.3
    Gene namesi
    Name:grpE
    Ordered Locus Names:b2614, JW2594
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10416. grpE.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731R → A: Great decrease in ability to interact with DnaK. 2 Publications
    Mutagenesisi74 – 741R → A: Great decrease in ability to interact with DnaK. 2 Publications
    Mutagenesisi82 – 821K → A: Great decrease in ability to interact with DnaK. 2 Publications
    Mutagenesisi86 – 861F → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi104 – 1041R → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi107 – 1071E → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi108 – 1081V → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi122 – 1221G → D: Temperature-sensitive phenotype. 2 Publications
    Mutagenesisi149 – 1491L → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi151 – 1511P → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi155 – 1551Q → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi157 – 1571I → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi159 – 1591M → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi174 – 1741M → A: No effect in ability to interact with DnaK. 2 Publications
    Mutagenesisi183 – 1831R → A: Loss of ability to interact with DnaK. 3 Publications
    Mutagenesisi186 – 1861R → A: No effect in ability to interact with DnaK. 1 Publication
    Mutagenesisi189 – 1891M → A: No effect in ability to interact with DnaK. 1 Publication
    Mutagenesisi192 – 1921V → A: Loss of ability to interact with DnaK. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 197197Protein GrpEPRO_0000113782Add
    BLAST

    Proteomic databases

    PaxDbiP09372.
    PRIDEiP09372.

    2D gel databases

    SWISS-2DPAGEP09372.

    Expressioni

    Inductioni

    By the sigma(32) subunit of RNA polymerase.

    Gene expression databases

    GenevestigatoriP09372.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi851433. 1 interaction.
    DIPiDIP-6141N.
    IntActiP09372. 49 interactions.
    MINTiMINT-1225400.
    STRINGi511145.b2614.

    Structurei

    Secondary structure

    1
    197
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi39 – 8547
    Helixi88 – 903
    Helixi91 – 944
    Helixi96 – 10712
    Helixi117 – 13418
    Turni135 – 1384
    Beta strandi139 – 1424
    Beta strandi146 – 1483
    Beta strandi153 – 1619
    Beta strandi163 – 1653
    Beta strandi169 – 1757
    Beta strandi177 – 1804
    Beta strandi183 – 1864
    Beta strandi188 – 1947

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DKGX-ray2.80A/B1-197[»]
    DisProtiDP00103.
    ProteinModelPortaliP09372.
    SMRiP09372. Positions 34-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09372.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GrpE family.Curated

    Phylogenomic databases

    eggNOGiCOG0576.
    HOGENOMiHOG000252084.
    KOiK03687.
    OMAiHENWEKS.
    OrthoDBiEOG6FJNJ9.
    PhylomeDBiP09372.

    Family and domain databases

    Gene3Di2.30.22.10. 1 hit.
    3.90.20.20. 1 hit.
    HAMAPiMF_01151. GrpE.
    InterProiIPR000740. GrpE.
    IPR013805. GrpE_coiled_coil.
    IPR009012. GrpE_head.
    [Graphical view]
    PANTHERiPTHR21237. PTHR21237. 1 hit.
    PfamiPF01025. GrpE. 1 hit.
    [Graphical view]
    PRINTSiPR00773. GRPEPROTEIN.
    SUPFAMiSSF51064. SSF51064. 1 hit.
    PROSITEiPS01071. GRPE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P09372-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKVANLEAQ    50
    LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID 100
    SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD 150
    PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA 197
    Length:197
    Mass (Da):21,798
    Last modified:July 1, 1989 - v1
    Checksum:iCDC4CD9D08AD4BEF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07863 Genomic DNA. Translation: CAA30711.1.
    U00096 Genomic DNA. Translation: AAC75663.1.
    AP009048 Genomic DNA. Translation: BAA16498.1.
    PIRiS01240.
    RefSeqiNP_417104.1. NC_000913.3.
    YP_490836.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75663; AAC75663; b2614.
    BAA16498; BAA16498; BAA16498.
    GeneIDi12931622.
    947097.
    KEGGiecj:Y75_p2561.
    eco:b2614.
    PATRICi32120625. VBIEscCol129921_2711.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07863 Genomic DNA. Translation: CAA30711.1 .
    U00096 Genomic DNA. Translation: AAC75663.1 .
    AP009048 Genomic DNA. Translation: BAA16498.1 .
    PIRi S01240.
    RefSeqi NP_417104.1. NC_000913.3.
    YP_490836.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DKG X-ray 2.80 A/B 1-197 [» ]
    DisProti DP00103.
    ProteinModelPortali P09372.
    SMRi P09372. Positions 34-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 851433. 1 interaction.
    DIPi DIP-6141N.
    IntActi P09372. 49 interactions.
    MINTi MINT-1225400.
    STRINGi 511145.b2614.

    Chemistry

    ChEMBLi CHEMBL1293284.

    2D gel databases

    SWISS-2DPAGE P09372.

    Proteomic databases

    PaxDbi P09372.
    PRIDEi P09372.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75663 ; AAC75663 ; b2614 .
    BAA16498 ; BAA16498 ; BAA16498 .
    GeneIDi 12931622.
    947097.
    KEGGi ecj:Y75_p2561.
    eco:b2614.
    PATRICi 32120625. VBIEscCol129921_2711.

    Organism-specific databases

    EchoBASEi EB0411.
    EcoGenei EG10416. grpE.

    Phylogenomic databases

    eggNOGi COG0576.
    HOGENOMi HOG000252084.
    KOi K03687.
    OMAi HENWEKS.
    OrthoDBi EOG6FJNJ9.
    PhylomeDBi P09372.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10416-MONOMER.
    ECOL316407:JW2594-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P09372.
    PROi P09372.

    Gene expression databases

    Genevestigatori P09372.

    Family and domain databases

    Gene3Di 2.30.22.10. 1 hit.
    3.90.20.20. 1 hit.
    HAMAPi MF_01151. GrpE.
    InterProi IPR000740. GrpE.
    IPR013805. GrpE_coiled_coil.
    IPR009012. GrpE_head.
    [Graphical view ]
    PANTHERi PTHR21237. PTHR21237. 1 hit.
    Pfami PF01025. GrpE. 1 hit.
    [Graphical view ]
    PRINTSi PR00773. GRPEPROTEIN.
    SUPFAMi SSF51064. SSF51064. 1 hit.
    PROSITEi PS01071. GRPE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis and transcriptional regulation of the Escherichia coli grpE gene, encoding a heat shock protein."
      Lipinska B., King J., Ang D., Georgopoulos C.
      Nucleic Acids Res. 16:7545-7562(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B178.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK."
      Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M.
      Proc. Natl. Acad. Sci. U.S.A. 88:2874-2878(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE FUNCTION.
    6. "Structure-function analysis of the Escherichia coli GrpE heat shock protein."
      Wu B., Wawrzynow A., Zylicz M., Georgopoulos C.
      EMBO J. 15:4806-4816(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "A GrpE mutant containing the NH(2)-terminal 'tail' region is able to displace bound polypeptide substrate from DnaK."
      Mehl A.F., Heskett L.D., Neal K.M.
      Biochem. Biophys. Res. Commun. 282:562-569(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE ROLE IN PEPTIDE RELEASE FROM DNAK.
    9. "Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures."
      Grimshaw J.P., Jelesarov I., Siegenthaler R.K., Christen P.
      J. Biol. Chem. 278:19048-19053(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE ROLE AS A THERMOSENSOR.
    10. Cited for: ROLE IN DNAK INTERACTION WITH SUBSTRATE.
    11. "Thermodynamic linkage in the GrpE nucleotide exchange factor, a molecular thermosensor."
      Gelinas A.D., Toth J., Bethoney K.A., Langsetmo K., Stafford W.F., Harrison C.J.
      Biochemistry 42:9050-9059(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-86; ARG-183 AND VAL-192.
    12. "Mutational analysis of the energetics of the GrpE.DnaK binding interface: equilibrium association constants by sedimentation velocity analytical ultracentrifugation."
      Gelinas A.D., Toth J., Bethoney K.A., Stafford W.F., Harrison C.J.
      J. Mol. Biol. 339:447-458(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-73; ARG-74; LYS-82; ARG-104; GLU-107; VAL-108; LEU-149; PRO-151; GLN-155; ILE-157; MET-159; MET-174; ARG-183 AND VAL-192.
    13. "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
      Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
      Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ATPASE DOMAIN OF DNAK, MUTAGENESIS OF GLY-122.

    Entry informationi

    Entry nameiGRPE_ECOLI
    AccessioniPrimary (citable) accession number: P09372
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 131 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, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3