In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. Predominantly detected in the cytoplasm. A number of isoforms are produced. According to EST sequences. Knockout mutation impairs stomatal closure and accelerates wilting, enhances sensitivity to heat treatment, and strengthens tolerance to potyvirus TuMV infection. Belongs to the heat shock protein 70 (TC 1.A.33) family. HSP110/SSE subfamily.