Reviewed, UniProtKB/Swiss-Prot P09372 (GRPE_ECOLI)

Names and origin

Protein names

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

Gene names

Name:	grpE
Ordered Locus Names:	b2614, JW2594

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.7 Ref.9
Subunit structure	Homodimer. HAMAP MF_01151
Subcellular location	Cytoplasm Probable.
Induction	By the sigma(32) subunit of RNA polymerase. HAMAP 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
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	adenyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro chaperone binding Inferred from electronic annotation. Source: InterPro protein homodimerization 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 MF_01151

PRO_0000113782

Sites

Site

183

1

Interaction with dnaK HAMAP MF_01151

Experimental info

Mutagenesis

73

1

R → A: Great decrease in ability to interact with dnaK. Ref.11

Mutagenesis

74

1

R → A: Great decrease in ability to interact with dnaK. Ref.11

Mutagenesis

82

1

K → A: Great decrease in ability to interact with dnaK. Ref.11

Mutagenesis

86

1

F → A: No effect in ability to interact with dnaK. Ref.10

Mutagenesis

104

1

R → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

107

1

E → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

108

1

V → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

122

1

G → D: Temperature-sensitive phenotype. Ref.12

Mutagenesis

149

1

L → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

151

1

P → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

155

1

Q → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

157

1

I → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

159

1

M → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

174

1

M → A: No effect in ability to interact with dnaK. Ref.11

Mutagenesis

183

1

R → A: Loss of ability to interact with dnaK. Ref.11 Ref.10

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.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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)
	P09372-1 [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: 3045760] [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: 9205837] [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: 9278503] [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: 16738553] [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: 1826368] [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: 8890154] [Abstract] Cited for: FUNCTION, MUTAGENESIS.
[7]	"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: 11401497] [Abstract] Cited for: POSSIBLE ROLE IN PEPTIDE RELEASE FROM DNAK.
[8]	"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: 12639955] [Abstract] Cited for: POSSIBLE ROLE AS A THERMOSENSOR.
[9]	"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: 15102842] [Abstract] Cited for: ROLE IN DNAK INTERACTION WITH SUBSTRATE.
[10]	"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: 12885238] [Abstract] Cited for: MUTAGENESIS OF PHE-86; ARG-183 AND VAL-192.
[11]	"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: 15136046] [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.
[12]	"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: 9103205] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ATPASE DOMAIN OF DNAK, MUTAGENESIS OF GLY-122.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X07863 Genomic DNA. Translation: CAA30711.1.
U00096 Genomic DNA. Translation: AAC75663.1.
AP009048 Genomic DNA. Translation: BAA16498.1.

PIR

S01240.

RefSeq

AP_003194.1.
NP_417104.1.

3D structure databases

PDBPDBe

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

DisProt

DP00103.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6141N.

STRING

P09372.

2-D gel databases

SWISS-2DPAGE

P09372.

ECO2DBASE

B025.3. 6TH EDITION.

Genome annotation databases

GeneID

947097.

GenomeReviews

Gene locus JW2594 in contig AP009048_GR.
Gene locus b2614 in contig U00096_GR.

KEGG

ecj:JW2594.
eco:b2614.

Organism-specific databases

EchoBASE

EB0411.

EcoGene

EG10416. grpE.

CMR

Search...

Phylogenomic databases

HOGENOM

P09372.

OMA

LHQAVMQ.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10416-MON.

Gene expression databases

Genevestigator

P09372.

Family and domain databases

HAMAP

MF_01151.
[Tree]

InterPro

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

Gene3D

G3DSA:3.90.20.20. GrpE_coiled_coil. 1 hit.
G3DSA:2.30.22.10. GrpE_head. 1 hit.

PANTHER

PTHR21237. GrpE. 1 hit.

Pfam

PF01025. GrpE. 1 hit.
[Graphical view]

PRINTS

PR00773. GRPEPROTEIN.

PROSITE

PS01071. GRPE. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	November 3, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)