Genome Property Definition Page

Namechaperone system: GroEL/GroES
DescriptionGroEL and GroES comprise the bacterial group I chaperonin, a toroidal complex involved in folding or refolding proteins in the cytosol. Archaea and Eukaryotes have instead (with a few rare cases of overlap) a group II chaperonin complex, usually called the thermosome in the Archaea and CCT in the Eukaryota. At least one member of the archaeal genus Methanosarcina, has both.
JCVI RoleProtein folding and stabilization
Parent PropertyGenProp0248: protein folding
Literature References
[ 1 ]Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL.  Structure and function in GroEL-mediated protein folding.  Annu Rev Biochem. 1998;67:581-608. Review.  PMID 9759498
[ 2 ]Klunker D, Haas B, Hirtreiter A, Figueiredo L, Naylor DJ, Pfeifer G, Muller V, Deppenmeier U, Gottschalk G, Hartl FU, Hayer-Hartl M.  Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei.  J Biol Chem. 2003 Aug 29;278(35):33256-67. Epub 2003 Jun 09.  PMID 12796498
Web ReferencesThe Ecocyc Database: Polypeptide: GroEL, chaperone Hsp60, peptide-dependent ATPase, heat shock protein
The Ecocyc Database: Polypeptide: GroES, 10 Kd chaperone binds to Hsp60 in pres. Mg-ATP, suppressing its ATPase activity
Gene Ontology TermGO:0006457: protein folding (biological_process)

Step NameStep NumRequiredEvidence (Method)Evidence Go Terms
chaperonin GroELGroELYESTIGR02348 (HMM): chaperonin GroLGO:0006457: protein folding
co-chaperonin GroESGroESYESPF00166 (HMM): chaperonin GroSGO:0006457: protein folding

Parent Properties
GenProp0248protein folding

Sibling Properties
GenProp0244chaperone system: DnaK-DnaJ-GrpE
GenProp0246chaperone system: thermosome/prefoldin
GenProp0725outer membrane protein assembly complex
GenProp0928OMP chaperone system: SurA-Skp-DegP