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PROSITE documentation PDOC00679 |
A number of ATP-binding proteins that are are thought to protect cells from extreme stress by controlling the aggregation of denaturation of vital cellular structures have been shown [1,2] to be evolutionary related. These proteins are listed below.
The size of these proteins range from 84 Kd (clpA) to slightly more than 100 Kd (HSP104). They all share two conserved regions of about 200 amino acids that each contains an ATP-binding site. In addition to the ATP-binding A and B motifs there are many parts in these two domains that are also conserved. We have selected two of these regions as signature patterns. The first signature is located in the first domain, some ten residues to the C-terminal of the ATP-binding B motif. The second pattern is located in the second domain in-between the ATP-binding A and B motifs.
Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Gottesman S. Squires C. Pichersky E. Carrington M. Hobbs M. Mattick J.S. Dalrymple B. Kuramitsu H. Shiroza T. Foster T. |
Title | Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990). | |
PubMed ID | 2185473 |
2 | Authors | Parsell D.A. Sanchez Y. Stitzel J.D. Lindquist S. |
Title | Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. | |
Source | Nature 353:270-273(1991). | |
PubMed ID | 1896074 | |
DOI | 10.1038/353270a0 |
3 | Authors | Leonhardt S.A. Fearson K. Danese P.N. Mason T.L. |
Title | HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. | |
Source | Mol. Cell. Biol. 13:6304-6313(1993). | |
PubMed ID | 8413229 |