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P09372 (GRPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 130. 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:
Protein GrpE
Alternative name(s):
HSP-70 cofactor
HSP24
Heat shock protein B25.3
Gene names
Name:grpE
Ordered Locus Names:b2614, JW2594
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.8 Ref.10

Subunit structure

Homodimer.

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_01151.

Induction

By the sigma32 subunit of RNA polymerase. HAMAP-Rule MF_01151

Sequence similarities

Belongs to the GrpE family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

protein unfolding

Inferred from direct assay PubMed 20953191. Source: EcoCyc

response to heat

Inferred from expression pattern PubMed 8349564. Source: EcoliWiki

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functionadenyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Protein GrpE HAMAP-Rule MF_01151
PRO_0000113782

Sites

Site1831Interaction with DnaK

Experimental info

Mutagenesis731R → A: Great decrease in ability to interact with DnaK. Ref.12
Mutagenesis741R → A: Great decrease in ability to interact with DnaK. Ref.12
Mutagenesis821K → A: Great decrease in ability to interact with DnaK. Ref.12
Mutagenesis861F → A: No effect in ability to interact with DnaK. Ref.11
Mutagenesis1041R → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1071E → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1081V → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1221G → D: Temperature-sensitive phenotype. Ref.13
Mutagenesis1491L → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1511P → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1551Q → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1571I → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1591M → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1741M → A: No effect in ability to interact with DnaK. Ref.12
Mutagenesis1831R → A: Loss of ability to interact with DnaK. Ref.11 Ref.12
Mutagenesis1861R → A: No effect in ability to interact with DnaK.
Mutagenesis1891M → A: No effect in ability to interact with DnaK.
Mutagenesis1921V → A: Loss of ability to interact with DnaK. Ref.11 Ref.12

Secondary structure

.......................... 197
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09372 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: CDC4CD9D08AD4BEF

FASTA19721,798
        10         20         30         40         50         60 
MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKVANLEAQ LAEAQTRERD 

        70         80         90        100        110        120 
GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV 

       130        140        150        160        170        180 
EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL 

       190 
NGRTIRAAMV TVAKAKA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Influence of GrpE on DnaK-substrate interactions."
Brehmer D., Gaessler C., Rist W., Mayer M.P., Bukau B.
J. Biol. Chem. 279:27957-27964(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07863 Genomic DNA. Translation: CAA30711.1.
U00096 Genomic DNA. Translation: AAC75663.1.
AP009048 Genomic DNA. Translation: BAA16498.1.
PIRS01240.
RefSeqNP_417104.1. NC_000913.3.
YP_490836.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DKGX-ray2.80A/B1-197[»]
DisProtDP00103.
ProteinModelPortalP09372.
SMRP09372. Positions 34-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid851433. 1 interaction.
DIPDIP-6141N.
IntActP09372. 49 interactions.
MINTMINT-1225400.
STRING511145.b2614.

Chemistry

ChEMBLCHEMBL1293284.

2D gel databases

SWISS-2DPAGEP09372.

Proteomic databases

PaxDbP09372.
PRIDEP09372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75663; AAC75663; b2614.
BAA16498; BAA16498; BAA16498.
GeneID12931622.
947097.
KEGGecj:Y75_p2561.
eco:b2614.
PATRIC32120625. VBIEscCol129921_2711.

Organism-specific databases

EchoBASEEB0411.
EcoGeneEG10416. grpE.

Phylogenomic databases

eggNOGCOG0576.
HOGENOMHOG000252084.
KOK03687.
OMAHENWEKS.
OrthoDBEOG6FJNJ9.
PhylomeDBP09372.

Enzyme and pathway databases

BioCycEcoCyc:EG10416-MONOMER.
ECOL316407:JW2594-MONOMER.

Gene expression databases

GenevestigatorP09372.

Family and domain databases

Gene3D2.30.22.10. 1 hit.
3.90.20.20. 1 hit.
HAMAPMF_01151. GrpE.
InterProIPR000740. GrpE.
IPR013805. GrpE_coiled_coil.
IPR009012. GrpE_head.
[Graphical view]
PANTHERPTHR21237. PTHR21237. 1 hit.
PfamPF01025. GrpE. 1 hit.
[Graphical view]
PRINTSPR00773. GRPEPROTEIN.
SUPFAMSSF51064. SSF51064. 1 hit.
PROSITEPS01071. GRPE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09372.
PROP09372.

Entry information

Entry nameGRPE_ECOLI
AccessionPrimary (citable) accession number: P09372
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 130 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene