The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. Members of the DnaJ family are characterized by the presence of the J domain. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. Proteins of the DnaJ family contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis.