{PDOC00576}
{PS00681; CHAPERONINS_CPN10}
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* Chaperonins cpn10 signature *
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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.

-Consensus pattern: [LIVMFY]-x-P-[ILT]-x-[DEN]-[KR]-[LIVMFA](3)-[KREQS]-
                    x(8,9)-[SG]-x-[LIVMFY](3)
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for 5 bacterial sequences.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note: 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.; georgopo@medecine.unige.ch

-Last update: December 2004 / Pattern and text revised.

[ 1] Ellis R.J., van der Vies S.M.
     "Molecular chaperones."
     Annu. Rev. Biochem. 60:321-347(1991).
     PubMed=1679318; DOI=10.1146/annurev.bi.60.070191.001541
[ 2] Zeilsta-Ryalls J., Fayet O., Georgopoulos C.
     Annu. Rev. Microbiol. 45:301-325(1991).
[ 3] Hartman D.J., Hoogenraad N.J., Condron R., Hoj P.B.
     "Identification of a mammalian 10-kDa heat shock protein, a
     mitochondrial chaperonin 10 homologue essential for assisted folding
     of trimeric ornithine transcarbamoylase in vitro."
     Proc. Natl. Acad. Sci. U.S.A. 89:3394-3398(1992).
     PubMed=1348860
[ 4] Bertsch U., Soll J., Seetharam R., Viitanen P.V.
     "Identification, characterization, and DNA sequence of a functional
     'double' groES-like chaperonin from chloroplasts of higher plants."
     Proc. Natl. Acad. Sci. U.S.A. 89:8696-8700(1992).
     PubMed=1356267
[ 5] Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J.
     "The crystal structure of the GroES co-chaperonin at 2.8 A
     resolution."
     Nature 379:37-45(1996).
     PubMed=8538739

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