chaperonin ATPase;
chaperonin

Hydrolases;
Acting on acid anhydrides;
Acting on acid anhydrides to facilitate cellular and subcellular movement

ATP phosphohydrolase (polypeptide-unfolding)

ATP + H2O = ADP + phosphate [RN:R00086]

R00086

ATP [CPD:C00002];
H2O [CPD:C00001]

Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 3.6.4.8 (proteasome ATPase).

1  [PMID:2897629]

Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ.

Homologous plant and bacterial proteins chaperone oligomeric protein assembly.

Nature. 333 (1988) 330-4.

Escherichia coli [GN:eco]

2  [PMID:2577724]

Lubben TH, Donaldson GK, Viitanen PV, Gatenby AA

Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone.

Plant. Cell. 1 (1989) 1223-30.

3

In: Ellis, R.J. (Ed.), The Chaperonins, Academic Press, San Diego, 1996.

4  [PMID:9657960]

Ranson NA, White HE, Saibil HR.

Chaperonins.

Biochem. J. 333 ( Pt 2) (1998) 233-42.

Escherichia coli [GN:eco]