{PDOC00269} {PS00297; HSP70_1} {PS00329; HSP70_2} {PS01036; HSP70_3} {BEGIN} *********************************************** * Heat shock hsp70 proteins family signatures * *********************************************** Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by the induction of the synthesis of proteins collectively known as heat-shock proteins (hsp) [1]. Amongst them is a family of proteins with an average molecular weight of 70 Kd, known as the hsp70 proteins [2,3,4]. In most species, there are many proteins that belong to the hsp70 family. Some of them are expressed under unstressed conditions. Hsp70 proteins can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc.). Some of the hsp70 family proteins are listed below: - In Escherichia coli and other bacteria, the main hsp70 protein is known as the dnaK protein. A second protein, hscA, has been recently discovered. dnaK is also found in the chloroplast genome of red algae. - In yeast, at least ten hsp70 proteins are known to exist: SSA1 to SSA4, SSB1, SSB2, SSC1, SSD1 (KAR2), SSE1 (MSI3) and SSE2. - In Drosophila, there are at least eight different hsp70 proteins: HSP70, HSP68, and HSC-1 to HSC-6. - In mammals, there are at least eight different proteins: HSPA1 to HSPA6, HSC70, and GRP78 (also known as the immunoglobulin heavy chain binding protein (BiP)). - In the sugar beet yellow virus (SBYV), a hsp70 homolog has been shown [5] to exist. - In archaebacteria, hsp70 proteins are also present [6]. All proteins belonging to the hsp70 family bind ATP. A variety of functions has been postulated for hsp70 proteins. It now appears [7] that some hsp70 proteins play an important role in the transport of proteins across membranes. They also seem to be involved in protein folding and in the assembly/ disassembly of protein complexes [8]. We have derived three signature patterns for the hsp70 family of proteins; the first centered on a conserved pentapeptide found in the N-terminal section of these proteins; the two others on conserved regions located in the central part of the sequence. -Consensus pattern: [IV]-D-L-G-T-[ST]-x-[SC] -Sequences known to belong to this class detected by the pattern: ALL, except for 16 sequences. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [LIVMF]-[LIVMFY]-[DN]-[LIVMFS]-G-[GSH]-[GS]-[AST]-x(3)- [ST]-[LIVM]-[LIVMFC] -Sequences known to belong to this class detected by the pattern: ALL, except for 7 sequences. -Other sequence(s) detected in Swiss-Prot: 1. -Consensus pattern: [LIVMY]-x-[LIVMF]-x-G-G-x-[ST]-{LS}-[LIVM]-P-x-[LIVM]-x- [DEQKRSTA] -Sequences known to belong to this class detected by the pattern: ALL, except for 4 sequences. -Other sequence(s) detected in Swiss-Prot: 6. -Expert(s) to contact by email: Genevaux P.; Pierre.Genevaux@ibcg.biotoul.fr -Last update: December 2004 / Pattern and text revised. [ 1] Lindquist S., Craig E.A. "The heat-shock proteins." Annu. Rev. Genet. 22:631-677(1988). PubMed=2853609; DOI=10.1146/annurev.ge.22.120188.003215 [ 2] Pelham H.R.B. "Speculations on the functions of the major heat shock and glucose-regulated proteins." Cell 46:959-961(1986). PubMed=2944601 [ 3] Pelham H. "Heat-shock proteins. Coming in from the cold." Nature 332:776-777(1988). PubMed=3282176; DOI=10.1038/332776a0 [ 4] Craig E.A. "Essential roles of 70kDa heat inducible proteins." BioEssays 11:48-52(1989). PubMed=2686623 [ 5] Agranovsky A.A., Boyko V.P., Karasev A.V., Koonin E.V., Dolja V.V. "Putative 65 kDa protein of beet yellows closterovirus is a homologue of HSP70 heat shock proteins." J. Mol. Biol. 217:603-610(1991). PubMed=2005613 [ 6] Gupta R.S., Singh B. "Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene." J. Bacteriol. 174:4594-4605(1992). PubMed=1624448 [ 7] Deshaies R.J., Koch B.D., Schekman R. "The role of stress proteins in membrane biogenesis." Trends Biochem. Sci. 13:384-388(1988). PubMed=3072700 [ 8] Craig E.A., Gross C.A. "Is hsp70 the cellular thermometer?" Trends Biochem. Sci. 16:135-140(1991). PubMed=1877088 -------------------------------------------------------------------------------- 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}