Isomerases;
Isomerases altering macromolecular conformation;
Enzymes altering polypeptide conformation or assembly
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ATP phosphohydrolase (polypeptide-unfolding)

ATP + H2O + an unfolded polypeptide = ADP + phosphate + a folded polypeptide

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

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 5.6.1.5 (proteasome ATPase).

EC 5.6.1.7 created 2000 as EC 3.6.4.9, transferred 2018 to EC 5.6.1.7

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 333:330-4 (1988)
DOI:10.1038/333330a0

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 1:1223-30 (1989)
DOI:10.1105/tpc.1.12.1223

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):233-42 (1998)
DOI:10.1042/bj3330233