ECOLI:CH60

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	groL (ECO:0000255 with HAMAP-Rule:MF_00600) (synonyms: groEL (ECO:0000255 with HAMAP-Rule:MF_00600), mopA)
Protein Name(s)	60 kDa chaperonin (ECO:0000255 with HAMAP-Rule:MF_00600) GroEL protein (ECO:0000255 with HAMAP-Rule:MF_00600) Protein Cpn60 (ECO:0000255 with HAMAP-Rule:MF_00600)
External Links
UniProt	P0A6F5
EMBL	X07850 U14003 U00096 AP009048 X07899 M11294
PIR	S56371
RefSeq	NP_418567.1 YP_492286.1
PDB	1AON 1DK7 1DKD 1FY9 1FYA 1GR5 1GRL 1GRU 1J4Z 1JON 1KID 1KP8 1KPO 1LA1 1MNF 1OEL 1PCQ 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK 2C7C 2C7D 2C7E 2CGT 2EU1 2NWC 2YEY 3C9V 3CAU 3VZ6 3VZ7 3VZ8 3WVL 3ZPZ 3ZQ0 3ZQ1 4AAQ 4AAR 4AAS 4AAU 4AB2 4AB3
PDBsum	1AON 1DK7 1DKD 1FY9 1FYA 1GR5 1GRL 1GRU 1J4Z 1JON 1KID 1KP8 1KPO 1LA1 1MNF 1OEL 1PCQ 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK 2C7C 2C7D 2C7E 2CGT 2EU1 2NWC 2YEY 3C9V 3CAU 3VZ6 3VZ7 3VZ8 3WVL 3ZPZ 3ZQ0 3ZQ1 4AAQ 4AAR 4AAS 4AAU 4AB2 4AB3
ProteinModelPortal	P0A6F5
SMR	P0A6F5
BioGrid	852957
DIP	DIP-339N
IntAct	P0A6F5
MINT	MINT-5232496
STRING	511145.b4143
SWISS-2DPAGE	P0A6F5
PaxDb	P0A6F5
PRIDE	P0A6F5
EnsemblBacteria	AAC77103 BAE78145
GeneID	12934083 948665
KEGG	ecj:Y75_p4030 eco:b4143
PATRIC	32123855
EchoBASE	EB0594
EcoGene	EG10599
eggNOG	COG0459
HOGENOM	HOG000076290
InParanoid	P0A6F5
KO	K04077
OMA	AAKMEWV
OrthoDB	EOG6JDWBZ
PhylomeDB	P0A6F5
BioCyc	EcoCyc:EG10599-MONOMER ECOL316407:JW4103-MONOMER
SABIO-RK	P0A6F5
EvolutionaryTrace	P0A6F5
PRO	PR:P0A6F5
Proteomes	UP000000318 UP000000625
Genevestigator	P0A6F5
GO	GO:0005829 GO:0016020 GO:0005524 GO:0016887 GO:0042802 GO:0051082 GO:0006200 GO:0007049 GO:0051301 GO:0006457 GO:0042026 GO:0009408 GO:0019068
Gene3D	1.10.560.10 3.50.7.10
HAMAP	MF_00600
InterPro	IPR018370 IPR001844 IPR002423 IPR027409 IPR027413
PANTHER	PTHR11353
Pfam	PF00118
PRINTS	PR00298
SUPFAM	SSF48592 SSF52029
TIGRFAMs	TIGR02348
PROSITE	PS00296

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
NOT\|involved_in	GO:0052212	modification of morphology or physiology of other organism via secreted substance involved in symbiotic interaction	PMID:11333970^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:1990220	GroEL-GroES complex	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10599 PANTHER:PTN000143644	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	EcoGene:EG10599 PANTHER:PTN000143677 SGD:S000004249	F	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000143677 SGD:S000004249	P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9878052^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:8618836^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:7935790^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22575645^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18568038^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18334219^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17098196^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6F5	F	Seeded From UniProt	complete
involved_in	GO:0019068	virion assembly	PMID:7015340^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:379350^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:8349564^[13]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:1990220	GroEL-GroES complex	PMID:9285585^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:10532860^[15]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:7935796^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:8097882^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:7935790^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:379350^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:2573517^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[20]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:9285585^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:8564544^[21]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:8564544^[21]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002423 InterPro:IPR018370	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001844 InterPro:IPR018370	C	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:IPR018370	P	Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001844	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000098153	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:UR000098153	C	Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000098153	P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000098153	F	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P	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
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
	GO:0031135	negative regulation of conjugation	PMID:17586648^[22]	ECO:0000315			P	Fig 2 shows that cells carrying the groEL allele gained full transfer competence 90 mins after the heat shock while wild type cells gained full transfer competence after 180 min after the heat shock.	complete
	GO:0031648	protein destabilization	PMID:17586648^[22]	ECO:0000315			P	See Fig 5	complete
	GO:1990220	GroEL-GroES complex	PMID:23437010^[23]	ECO:0000314			C	See Figure 1 of associated PMID	complete CACAO 9575
	GO:0071218	cellular response to misfolded protein	PMID:15866952^[24]	ECO:0000314			P	Figure 1. Shows a cellular response to misfolded protein aggregation via localization of the GroEL chaperone system to the β-galactosidase fusion protein VP1LAC aggreagate in the cytoplasm	complete
	GO:0005737	cytoplasm	PMID:15866952^[24]	ECO:0000314			C	Figure 1. shows GroEl chaperone system localization to aggregation-prone β-galactosidase fusion protein VP1LAC in the cytoplasm.	complete
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Notes

References

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

↑ Yoshida, N et al. (2001) Protein function. Chaperonin turned insect toxin. Nature 411 44 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 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
↑ ^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
↑ Siegers, K et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18 75-84 PubMed GONUTS page
↑ Azem, A et al. (1995) The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. Proc. Natl. Acad. Sci. U.S.A. 92 12021-5 PubMed GONUTS page
↑ ^6.0 ^6.1 Braig, K et al. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371 578-86 PubMed GONUTS page
↑ Chen, J et al. (2012) Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone. FEBS Lett. 586 1120-7 PubMed GONUTS page
↑ Katayama, H et al. (2008) GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore. Nat. Struct. Mol. Biol. 15 754-60 PubMed GONUTS page
↑ Ludtke, SJ et al. (2008) De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 16 441-8 PubMed GONUTS page
↑ Chen, DH et al. (2006) An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate. Structure 14 1711-22 PubMed GONUTS page
↑ Tilly, K et al. (1981) Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc. Natl. Acad. Sci. U.S.A. 78 1629-33 PubMed GONUTS page
↑ ^12.0 ^12.1 Hendrix, RW (1979) Purification and properties of groE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129 375-92 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
↑ ^14.0 ^14.1 Xu, Z et al. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 741-50 PubMed GONUTS page
↑ Goloubinoff, P et al. () Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342 884-9 PubMed GONUTS page
↑ Fenton, WA et al. (1994) Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371 614-9 PubMed GONUTS page
↑ Braig, K et al. (1993) A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proc. Natl. Acad. Sci. U.S.A. 90 3978-82 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Kusukawa, N et al. (1989) Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 8 3517-21 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ ^21.0 ^21.1 Boisvert, DC et al. (1996) The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nat. Struct. Biol. 3 170-7 PubMed GONUTS page
↑ ^22.0 ^22.1 Zahrl, D et al. (2007) GroEL plays a central role in stress-induced negative regulation of bacterial conjugation by promoting proteolytic degradation of the activator protein TraJ. J. Bacteriol. 189 5885-94 PubMed GONUTS page
↑ Wang, Y et al. (2013) Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622. PLoS Genet. 9 e1003306 PubMed GONUTS page
↑ ^24.0 ^24.1 Carrió, MM & Villaverde, A (2005) Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187 3599-601 PubMed GONUTS page

[PMID:11333970-1] Yoshida, N et al. (2001) Protein function. Chaperonin turned insect toxin. Nature 411 44 PubMed GONUTS page

[PMID:16858726-2] 2.0 ^2.1 ^2.2 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:9878052-4] Siegers, K et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18 75-84 PubMed GONUTS page

[PMID:8618836-5] Azem, A et al. (1995) The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer. Proc. Natl. Acad. Sci. U.S.A. 92 12021-5 PubMed GONUTS page

[PMID:7935790-6] 6.0 ^6.1 Braig, K et al. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371 578-86 PubMed GONUTS page

[PMID:22575645-7] Chen, J et al. (2012) Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone. FEBS Lett. 586 1120-7 PubMed GONUTS page

[PMID:18568038-8] Katayama, H et al. (2008) GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore. Nat. Struct. Mol. Biol. 15 754-60 PubMed GONUTS page

[PMID:18334219-9] Ludtke, SJ et al. (2008) De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 16 441-8 PubMed GONUTS page

[PMID:17098196-10] Chen, DH et al. (2006) An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate. Structure 14 1711-22 PubMed GONUTS page

[PMID:7015340-11] Tilly, K et al. (1981) Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc. Natl. Acad. Sci. U.S.A. 78 1629-33 PubMed GONUTS page

[PMID:379350-12] 12.0 ^12.1 Hendrix, RW (1979) Purification and properties of groE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129 375-92 PubMed GONUTS page

[PMID:8349564-13] 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:9285585-14] 14.0 ^14.1 Xu, Z et al. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 741-50 PubMed GONUTS page

[PMID:10532860-15] Goloubinoff, P et al. () Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342 884-9 PubMed GONUTS page

[PMID:7935796-16] Fenton, WA et al. (1994) Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371 614-9 PubMed GONUTS page

[PMID:8097882-17] Braig, K et al. (1993) A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proc. Natl. Acad. Sci. U.S.A. 90 3978-82 PubMed GONUTS page

[PMID:27718375-18] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:2573517-19] Kusukawa, N et al. (1989) Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 8 3517-21 PubMed GONUTS page

[PMID:18304323-20] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:8564544-21] 21.0 ^21.1 Boisvert, DC et al. (1996) The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nat. Struct. Biol. 3 170-7 PubMed GONUTS page

[PMID:17586648-22] 22.0 ^22.1 Zahrl, D et al. (2007) GroEL plays a central role in stress-induced negative regulation of bacterial conjugation by promoting proteolytic degradation of the activator protein TraJ. J. Bacteriol. 189 5885-94 PubMed GONUTS page

[PMID:23437010-23] Wang, Y et al. (2013) Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622. PLoS Genet. 9 e1003306 PubMed GONUTS page

[PMID:15866952-24] 24.0 ^24.1 Carrió, MM & Villaverde, A (2005) Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187 3599-601 PubMed GONUTS page

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ECOLI:CH60

Contents

Annotations

Notes

References

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