Function and Biology

GroEL:GroES-ATP complex under continuous turnover conditions

Source organism: Escherichia coli
Biochemical function: unfolded protein binding
Biological process: chaperone cofactor-dependent protein refolding
Cellular component: GroEL-GroES complex

EC 5.6.1.7: Chaperonin ATPase

Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Systematic name:
ATP phosphohydrolase (polypeptide-unfolding)
Alternative Name(s):
  • Chaperonin

Sequence families

Pfam Protein families (Pfam)
PF00166
Domain description: Chaperonin 10 Kd subunit
Occurring in:
  1. Co-chaperonin GroES
The deposited structure of PDB entry 8bkz contains 14 copies of Pfam domain PF00166 (Chaperonin 10 Kd subunit) in Co-chaperonin GroES. Showing 1 copy in chain Z [auth AA].

PF00118
Domain description: TCP-1/cpn60 chaperonin family
Occurring in:
  1. Chaperonin GroEL
The deposited structure of PDB entry 8bkz contains 14 copies of Pfam domain PF00118 (TCP-1/cpn60 chaperonin family) in Chaperonin GroEL. Showing 1 copy in chain C [auth A].