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ECOLI:CH10

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) groS (synonyms: groES, mopB)
Protein Name(s) 10 kDa chaperonin

GroES protein Protein Cpn10

External Links
UniProt P0A6F9
EMBL X07850
X07899
U14003
U00096
AP009048
PIR S03931
RefSeq NP_418566.1
YP_492285.1
PDB 1AON
1EGS
1GRU
1PCQ
1PF9
1SVT
1SX4
2C7C
2C7D
3WVL
3ZPZ
3ZQ0
3ZQ1
PDBsum 1AON
1EGS
1GRU
1PCQ
1PF9
1SVT
1SX4
2C7C
2C7D
3WVL
3ZPZ
3ZQ0
3ZQ1
ProteinModelPortal P0A6F9
SMR P0A6F9
DIP DIP-9835N
IntAct P0A6F9
MINT MINT-5232475
STRING 511145.b4142
PhosSite P0809397
SWISS-2DPAGE P0A6F9
PaxDb P0A6F9
PRIDE P0A6F9
EnsemblBacteria AAC77102
BAE78144
GeneID 12933204
948655
KEGG ecj:Y75_p4029
eco:b4142
PATRIC 32123853
EchoBASE EB0595
EcoGene EG10600
eggNOG COG0234
HOGENOM HOG000133897
InParanoid P0A6F9
KO K04078
OMA GYGVKVE
OrthoDB EOG6GFGSD
PhylomeDB P0A6F9
BioCyc EcoCyc:EG10600-MONOMER
ECOL316407:JW4102-MONOMER
SABIO-RK P0A6F9
EvolutionaryTrace P0A6F9
PRO PR:P0A6F9
Proteomes UP000000318
UP000000625
Genevestigator P0A6F9
GO GO:0005829
GO:0005524
GO:0042802
GO:0051082
GO:0007049
GO:0051301
GO:0006457
GO:0009408
GO:0019068
Gene3D 2.30.33.40
HAMAP MF_00580
InterPro IPR020818
IPR018369
IPR011032
PANTHER PTHR10772
Pfam PF00166
PRINTS PR00297
SMART SM00883
SUPFAM SSF50129
PROSITE PS00681

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006457

protein folding

PMID:2192863[1]

ECO:0000314

P

Figure 2a shows the effect of addition of GroES and ATP to a arrested GroEL protein folding of pre-beta-lactamase. Enzyme function dramatically increases after addition,suggesting GroES is required for proper protein folding

complete
CACAO 8869

GO:0006457

protein folding

PMID:7901771[2]

ECO:0000314

P

Fig 1-B shows the competition between groS and groL for unlabelled ATP and binding at varying temperatures.

complete
CACAO 9613

involved_in

GO:0006457

protein folding

PMID:2192863[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051087

chaperone binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000080668
SGD:S000005546
UniProtKB:P61604
UniProtKB:Q8IDZ8

F

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10600
PANTHER:PTN000080668

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000080668
SGD:S000005546

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000080668
UniProtKB:P9WPE5

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6F9

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:10077571[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6F9

F

Seeded From UniProt

complete

involved_in

GO:0019068

virion assembly

PMID:7015340[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

Contributes to

GO:0019835

cytolysis

PMID:16030234[7]

ECO:0000315

P

Figure 4 shows E. coli with mutations to groES that impact the ability of phage PRD1 to lyse the host bacteria. Temperature sensitive mutants, closed triangle, groES mutant DW719(pLM2), lost cytolysis at 40 degrees. The wt closed circle wt strain DW720(pLM2), does not lose cytolysis at 40 degrees. This shows loss of cytolysis when the temperature is raised with this gene and the normal lysis in the wt as control.

complete
CACAO 12888

involved_in

GO:0009408

response to heat

PMID:8349564[8]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:1990220

GroEL-GroES complex

PMID:9285585[9]

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[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:3017973[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:2573517[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018369

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:IPR037124

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:IPR018369
InterPro:IPR020818
InterPro:IPR037124

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000030636

C

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000030636

P

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

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

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Laminet, AA et al. (1990) The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J. 9 2315-9 PubMed GONUTS page
  2. ↑ Martin, J et al. (1993) Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES. Nature 366 279-82 PubMed GONUTS page
  3. ↑ 3.0 3.1 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
  4. ↑ 4.0 4.1 4.2 4.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. ↑ Horowitz, PM et al. (1999) GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism. Proc. Natl. Acad. Sci. U.S.A. 96 2682-6 PubMed GONUTS page
  6. ↑ 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
  7. ↑ Ziedaite, G et al. (2005) The Holin protein of bacteriophage PRD1 forms a pore for small-molecule and endolysin translocation. J. Bacteriol. 187 5397-405 PubMed GONUTS page
  8. ↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
  9. ↑ Xu, Z et al. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 741-50 PubMed GONUTS page
  10. ↑ 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
  11. ↑ Chandrasekhar, GN et al. (1986) Purification and properties of the groES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261 12414-9 PubMed GONUTS page
  12. ↑ 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
  13. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  14. ↑ 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
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