PROSITE documentation PDOC00822 [for PROSITE entry PS01071]grpE protein signature
In prokaryotes the grpE protein [1] 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 [2] 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: Last update:December 2004 / Pattern and text revised.
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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). | |
| PubMed ID | 8280473 | |
| DOI | 10.1146/annurev.cb.09.110193.003125 |
| 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). | |
| PubMed ID | 8168496 |
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