P09372 (GRPE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein GrpE

Alternative name(s):
HSP-70 cofactor
HSP24
Heat shock protein B25.3

Gene names

Name:	grpE
Ordered Locus Names:	b2614, JW2594

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Stress response
Cellular component	Cytoplasm
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein 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_component	cytoplasm Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	adenyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 197

197

Protein GrpE HAMAP-Rule MF_01151

PRO_0000113782

Sites

Site

183

1

Interaction with DnaK

Experimental info

Mutagenesis

73

1

R → A: Great decrease in ability to interact with DnaK. Ref.12

Mutagenesis

74

1

R → A: Great decrease in ability to interact with DnaK. Ref.12

Mutagenesis

82

1

K → A: Great decrease in ability to interact with DnaK. Ref.12

Mutagenesis

86

1

F → A: No effect in ability to interact with DnaK. Ref.11

Mutagenesis

104

1

R → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

107

1

E → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

108

1

V → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

122

1

G → D: Temperature-sensitive phenotype. Ref.13

Mutagenesis

149

1

L → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

151

1

P → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

155

1

Q → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

157

1

I → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

159

1

M → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

174

1

M → A: No effect in ability to interact with DnaK. Ref.12

Mutagenesis

183

1

R → A: Loss of ability to interact with DnaK. Ref.11 Ref.12

Mutagenesis

186

1

R → A: No effect in ability to interact with DnaK.

Mutagenesis

189

1

M → A: No effect in ability to interact with DnaK.

Mutagenesis

192

1

V → A: Loss of ability to interact with DnaK. Ref.11 Ref.12

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

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197

Helix Strand Turn

Details...

Helix

39 – 85

47

Helix

88 – 90

3

Helix

91 – 94

4

Helix

96 – 107

12

Helix

117 – 134

18

Turn

135 – 138

4

Beta strand

139 – 142

4

Beta strand

146 – 148

3

Beta strand

153 – 161

9

Beta strand

163 – 165

3

Beta strand

169 – 175

7

Beta strand

177 – 180

4

Beta strand

183 – 186

4

Beta strand

188 – 194

7

Sequences

	Sequence		Length	Mass (Da)
	P09372 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: CDC4CD9D08AD4BEF	FASTA	197	21,798
	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

References

	« Hide 'large scale' referencesShow '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. , 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 277:1453-1474(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.

PIR

S01240.

RefSeq

NP_417104.1. NC_000913.2.
YP_490836.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DKG	X-ray	2.80	A/B	1-197	[»]

DisProt

DP00103.

ProteinModelPortal

P09372.

SMR

P09372. Positions 34-197.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6141N.

IntAct

P09372. 49 interactions.

MINT

MINT-1225400.

STRING

511145.b2614.

2D gel databases

SWISS-2DPAGE

P09372.

Proteomic databases

PaxDb

P09372.

PRIDE

P09372.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75663; AAC75663; b2614.
BAA16498; BAA16498; BAA16498.

GeneID

12931622.
947097.

KEGG

ecj:Y75_p2561.
eco:b2614.

PATRIC

32120625. VBIEscCol129921_2711.

Organism-specific databases

EchoBASE

EB0411.

EcoGene

EG10416. grpE.

Phylogenomic databases

eggNOG

COG0576.

HOGENOM

HOG000252084.

KO

K03687.

OMA

DEHPADT.

ProtClustDB

PRK10325.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P09372.

Family and domain databases

Gene3D

2.30.22.10. 1 hit.
3.90.20.20. 1 hit.

HAMAP

MF_01151. GrpE.

InterPro

IPR000740. GrpE.
IPR013805. GrpE_coiled_coil.
IPR009012. GrpE_head.
[Graphical view]

PANTHER

PTHR21237. PTHR21237. 1 hit.

Pfam

PF01025. GrpE. 1 hit.
[Graphical view]

PRINTS

PR00773. GRPEPROTEIN.

SUPFAM

SSF51064. GrpE_head. 1 hit.

PROSITE

PS01071. GRPE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1293284.

EvolutionaryTrace

P09372.

Entry information

Entry name

GRPE_ECOLI

Accession

Primary (citable) accession number: P09372

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program