PROSITE documentation PDOC00576
Chaperonins cpn10 signature


Chaperonins [1,2] are proteins involved in the folding of proteins or the assembly of oligomeric protein complexes. They seem to assist other polypeptides in maintaining or assuming 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 cpn10 protein binds to cpn60 in the presence of MgATP and suppresses the ATPase activity of the latter. Cpn10 is a protein of about 100 amino acid residues whose sequence is well conserved in bacteria, vertebrate mitochondria and plants chloroplast [3,4]. Cpn10 assembles as an heptamer that forms a dome [5]. As a signature pattern for cpn10 we selected a region located in the N-terminal section of the protein.


This pattern is found twice in the plant chloroplast protein which consist of the tandem repeat of a cpn10 domain.

Expert(s) to contact by email:

Georgopoulos C.

Last update:

December 2004 / Pattern and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

CHAPERONINS_CPN10, PS00681; Chaperonins cpn10 signature  (PATTERN)


1AuthorsEllis R.J. van der Vies S.M.
TitleMolecular chaperones.
SourceAnnu. Rev. Biochem. 60:321-347(1991).
PubMed ID1679318

2AuthorsZeilsta-Ryalls J. Fayet O. Georgopoulos C.
SourceAnnu. Rev. Microbiol. 45:301-325(1991).

3AuthorsHartman D.J. Hoogenraad N.J. Condron R. Hoj P.B.
TitleIdentification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro.
SourceProc. Natl. Acad. Sci. U.S.A. 89:3394-3398(1992).
PubMed ID1348860

4AuthorsBertsch U. Soll J. Seetharam R. Viitanen P.V.
TitleIdentification, characterization, and DNA sequence of a functional 'double' groES-like chaperonin from chloroplasts of higher plants.
SourceProc. Natl. Acad. Sci. U.S.A. 89:8696-8700(1992).
PubMed ID1356267

5AuthorsHunt J.F. Weaver A.J. Landry S.J. Gierasch L. Deisenhofer J.
TitleThe crystal structure of the GroES co-chaperonin at 2.8 A resolution.
SourceNature 379:37-45(1996).
PubMed ID8538739

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