|PROSITE documentation PDOC00822 [for PROSITE entry PS01071]|
In prokaryotes the grpE protein  stimulates, jointly with dnaJ, the ATPase activity of the dnaK chaperone. It seems to accelerate the release of ADP from dnaK thus allowing dnaK to recycle more efficiently. GrpE is a protein of about 22 to 25 Kd. In yeast, an evolutionary related mitochondrial protein (gene GRPE) has been shown  to associate with the mitochondrial hsp70 protein and to thus play a role in the import of proteins from the cytoplasm.
As a signature pattern, we selected the most conserved region of grpE. It is located in the C-terminal section.Expert(s) to contact by email:
December 2004 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Georgopoulos C. Welch W.J.|
|Title||Role of the major heat shock proteins as molecular chaperones.|
|Source||Annu. Rev. Cell Biol. 9:601-634(1993).|
|2||Authors||Bolliger L. Deloche O. Glick B.S. Georgopoulos C. Jeno P. Kronidou N. Horst M. Morishima N. Schatz G.|
|Title||A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability.|
|Source||EMBO J. 13:1998-2006(1994).|