| Literature References | 1. GEORGOPOULOS, C. AND WELCH, W.
Role of the major heat-shock proteins as molecular chaperones.
ANNU.REV.CELL BIOL. 9 601-635 (1993).
2. BOLLIGER, L., DELOCHE, O., GLICK, B.S., GEORGOPOULOS, C., JENOE, P.,
KRONIDOU, N., HORST, M., MORISHIMA, N. AND SCHATZ, G.
A mitochondrial homolog of bacterial grpE interacts with mitochondrial
hsp70 and is essential for viability.
EMBO J. 13 1998-2006 (1994).
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| Documentation | Acting in concert with dnaJ, the prokaryotic grpE protein stimulates
the ATPase activity of the dnaK chaperone [1]. The protein apparently
accelerate the release of ADP from dnaK, allowing dnaK to recycle more
efficiently. An evolutionarily related mitochondrial protein in yeast has
been shown to associate with the mitochondrial hsp70 protein; it thus
plays a role in the import of proteins from the cytoplasm [2].
GRPEPROTEIN is a 4-element fingerprint that provides a signature for the
grpE protein family. The fingerprint was derived from an initial alignment
of 9 sequences: the motifs were drawn from short conserved regions spanning
the full alignment length - motifs 3 and 4 span the region encoded by
PROSITE pattern GRPE (PS01071), which lies at the C-terminus. Two
iterations on OWL29.4 were required to reach convergence, at which point
a true set comprising 23 sequences was identified. Several partial matches
were also found, all of which are fragments and family members that fail
to make significant matches with one or more motifs.
An update on SPTR37_9f identified a true set of 32 sequences, and 4
partial matches.
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