The Heat Shock Protein 70 (Hsp70) superfamily of chaperones assist in numerous folding processes and are upregulated by heat stress and toxic chemicals. Hsp70 chaperones share a highly conserved bipartite domain structure composed of an ATPase domain and a substrate-binding domain. (Adapted from PMID:17441502, FBrf0232269 and FBrf0174945).
Notes on Group
Kaneko (2022, FBrf0253513) has further classified D. mel Hsp70s into cytosolic A, cytosolic B, ER, and mitochondrial linages based on phylogenetic analysis.
