{PDOC00679}
{PS00870; CLPAB_1}
{PS00871; CLPAB_2}
{BEGIN}
*********************************
* Chaperonins clpA/B signatures *
*********************************

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.

 - Escherichia  coli  clpA,  which acts as the  regulatory subunit of the ATP-
   dependent protease clp.
 - Rhodopseudomonas blastica clpA homolog.
 - Escherichia coli heat shock protein clpB and homologs in other bacteria.
 - Bacillus subtilis protein mecB.
 - Yeast heat shock protein 104 (gene HSP104), which is vital for tolerance to
   heat, ethanol and other stresses.
 - Neurospora heat shock protein hsp98.
 - Yeast mitochondrial heat shock protein 78 (gene HSP78) [3].
 - CD4A  and CD4b, two highly related  tomato proteins that seem to be located
   in the chloroplast.
 - Trypanosoma brucei protein clp.
 - Porphyra purpurea chloroplast encoded clpC.

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.

-Consensus pattern: [DA]-[AI]-[SGA]-[NQS]-[LIVMF](2)-K-[PT]-x-[LM]-x(2)-G
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [RGT]-[LIVMFY]-[DN]-x-[ST]-E-[LIVMFY]-x-[ED]-[KRQEAS]-x-
                    [STA]-x-[STAD]-[KRS]-[LIVM]-x-G-[STAP]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2006 / Pattern revised.

[ 1] Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
     Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.
     "Conservation of the regulatory subunit for the Clp ATP-dependent
     protease in prokaryotes and eukaryotes."
     Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
     PubMed=2185473
[ 2] Parsell D.A., Sanchez Y., Stitzel J.D., Lindquist S.
     "Hsp104 is a highly conserved protein with two essential
     nucleotide-binding sites."
     Nature 353:270-273(1991).
     PubMed=1896074; DOI=10.1038/353270a0
[ 3] Leonhardt S.A., Fearson K., Danese P.N., Mason T.L.
     "HSP78 encodes a yeast mitochondrial heat shock protein in the Clp
     family of ATP-dependent proteases."
     Mol. Cell. Biol. 13:6304-6313(1993).
     PubMed=8413229

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}