ECOLI:GRPE

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	grpE
Protein Name(s)	Protein GrpE HSP-70 cofactor HSP24 Heat shock protein B25.3
External Links
UniProt	P09372
EMBL	X07863 U00096 AP009048
PIR	S01240
RefSeq	NP_417104.1 YP_490836.1
PDB	1DKG
PDBsum	1DKG
DisProt	DP00103
ProteinModelPortal	P09372
SMR	P09372
BioGrid	851433
DIP	DIP-6141N
IntAct	P09372
MINT	MINT-1225400
STRING	511145.b2614
ChEMBL	CHEMBL1293284
SWISS-2DPAGE	P09372
PaxDb	P09372
PRIDE	P09372
EnsemblBacteria	AAC75663 BAA16498
GeneID	12931622 947097
KEGG	ecj:Y75_p2561 eco:b2614
PATRIC	32120625
EchoBASE	EB0411
EcoGene	EG10416
eggNOG	COG0576
HOGENOM	HOG000252084
InParanoid	P09372
KO	K03687
OMA	DQFLRAK
OrthoDB	EOG6FJNJ9
PhylomeDB	P09372
BioCyc	EcoCyc:EG10416-MONOMER ECOL316407:JW2594-MONOMER
EvolutionaryTrace	P09372
PRO	PR:P09372
Proteomes	UP000000318 UP000000625
Genevestigator	P09372
GO	GO:0005737 GO:0000774 GO:0006457 GO:0043335 GO:0009408
Gene3D	2.30.22.10 3.90.20.20
HAMAP	MF_01151
InterPro	IPR000740 IPR013805 IPR009012
PANTHER	PTHR21237
Pfam	PF01025
PRINTS	PR00773
SUPFAM	SSF51064
PROSITE	PS01071

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0000774	adenyl-nucleotide exchange factor activity	PMID:9103205^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9103205^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:9103205^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6Y8	F	Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:9103205^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:9103205^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1334416 PANTHER:PTN000478264 UniProtKB:Q9HAV7	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10416 PANTHER:PTN000478395	C	Seeded From UniProt	complete
enables	GO:0000774	adenyl-nucleotide exchange factor activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10416 PANTHER:PTN000478264 SGD:S000005758	F	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:8349564^[4]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:11084044^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0000774	adenyl-nucleotide exchange factor activity	PMID:8599944^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000774	adenyl-nucleotide exchange factor activity	PMID:1826368^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0000774	P	Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000774	P	Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000774	P	Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000774	P	Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000774	P	Seeded From UniProt	complete
enables	GO:0000774	adenyl-nucleotide exchange factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000740	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000740 InterPro:IPR009012	P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000740	F	Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000740	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000164509	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Harrison, CJ et al. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276 431-5 PubMed GONUTS page
↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
↑ Grimshaw, JP et al. (2001) Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem. 276 6098-104 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Gamer, J et al. (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15 607-17 PubMed GONUTS page
↑ Liberek, K et al. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. U.S.A. 88 2874-8 PubMed GONUTS page

[PMID:9103205-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Harrison, CJ et al. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276 431-5 PubMed GONUTS page

[PMID:16858726-2] Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:21873635-3] 3.0 ^3.1 ^3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8349564-4] Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page

[PMID:11084044-5] Grimshaw, JP et al. (2001) Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem. 276 6098-104 PubMed GONUTS page

[PMID:18304323-6] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-7] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:8599944-8] Gamer, J et al. (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15 607-17 PubMed GONUTS page

[PMID:1826368-9] Liberek, K et al. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. U.S.A. 88 2874-8 PubMed GONUTS page

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ECOLI:GRPE

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