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Protein

Protein GrpE

Gene

grpE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • protein folding Source: InterPro
  • protein unfolding Source: EcoCyc
  • response to heat Source: EcoliWiki
Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10416. grpE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

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

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 – 8547Combined sources
Helixi88 – 903Combined sources
Helixi91 – 944Combined sources
Helixi96 – 10712Combined sources
Helixi117 – 13418Combined sources
Turni135 – 1384Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi153 – 1619Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi169 – 1757Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi188 – 1947Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP09372.
KOiK03687.
OMAiESFDHNL.
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

        10         20         30         40         50
MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKVANLEAQ
60 70 80 90 100
LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID
110 120 130 140 150
SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD
160 170 180 190
PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA
Length:197
Mass (Da):21,798
Last modified:July 1, 1989 - v1
Checksum:iCDC4CD9D08AD4BEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001393454.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75663; AAC75663; b2614.
BAA16498; BAA16498; BAA16498.
GeneIDi947097.
KEGGieco:b2614.
PATRICi32120625. VBIEscCol129921_2711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001393454.1. NZ_CP010445.1.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL1293284.

2D gel databases

SWISS-2DPAGEP09372.

Proteomic databases

PaxDbiP09372.
PRIDEiP09372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75663; AAC75663; b2614.
BAA16498; BAA16498; BAA16498.
GeneIDi947097.
KEGGieco:b2614.
PATRICi32120625. VBIEscCol129921_2711.

Organism-specific databases

EchoBASEiEB0411.
EcoGeneiEG10416. grpE.

Phylogenomic databases

eggNOGiCOG0576.
HOGENOMiHOG000252084.
InParanoidiP09372.
KOiK03687.
OMAiESFDHNL.
OrthoDBiEOG6FJNJ9.
PhylomeDBiP09372.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP09372.
PROiP09372.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.