Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. Interacts with HRAS. Interacts with HBV protein X and HTLV-1 protein p40tax. Belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB.
Molecular Function: apolipoprotein A-I binding; apolipoprotein binding; ATPase activity; chaperone binding; DNA replication origin binding; double-stranded RNA binding; enzyme binding; high-density lipoprotein binding; lipopolysaccharide binding; p53 binding; protein binding; RNA binding; single-stranded DNA binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: 'de novo' protein folding; adhesion to host; apoptotic mitochondrial changes; B cell activation; B cell cytokine production; B cell proliferation; caspase activation; chaperone-mediated protein complex assembly; interaction with symbiont; isotype switching to IgG isotypes; MyD88-dependent toll-like receptor signaling pathway; negative regulation of apoptosis; positive regulation of apoptosis; positive regulation of interferon-alpha production; positive regulation of interferon-gamma production; positive regulation of interleukin-10 production; positive regulation of interleukin-12 production; positive regulation of interleukin-6 production; positive regulation of macrophage activation; positive regulation of T cell activation; positive regulation of T cell mediated immune response to tumor cell; protein import into mitochondrial intermembrane space; protein maturation; protein refolding; protein stabilization; regulation of transcription from RNA polymerase II promoter; response to cold; response to unfolded protein; T cell activation