|PROSITE documentation PDOC00268 [for PROSITE entry PS00296]|
Chaperonins [1,2] are proteins involved in the folding of proteins or the assembly of oligomeric protein complexes. Their role seems to be to assist other polypeptides to maintain or assume conformations which permit their correct assembly into oligomeric structures. They are found in abundance in prokaryotes, chloroplasts and mitochondria. Chaperonins form oligomeric complexes and are composed of two different types of subunits: a 60 Kd protein, known as cpn60 (groEL in bacteria) and a 10 Kd protein, known as cpn10 (groES in bacteria).
The cpn60 protein shows weak ATPase activity and is a highly conserved protein of about 550 to 580 amino acid residues which has been described by different names in different species:
As a signature pattern for these proteins, we have chosen a rather well conserved region of twelve residues, located in the last third of the cpn60 sequence.Expert(s) to contact by email:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Ellis R.J. van der Vies S.M.|
|Source||Annu. Rev. Biochem. 60:321-347(1991).|
|2||Authors||Zeilsta-Ryalls J. Fayet O. Georgopoulos C.|
|Source||Annu. Rev. Microbiol. 45:301-325(1991).|