HSP40/DnaJ peptide-binding

Definition

The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at intermediate stages of folding, assembly, and translocation across membranes PMID:9600925. Binding of protein substrates to the DnaK C-terminal domain is controlled by ATP binding and hydrolysis in the N-terminal ATPase domain. The interaction of DnaJ with DnaK is mediated at least in part by the highly conserved N-terminal J-domain of DnaJ. The J-domain interaction is localized to the ATPase domain of DnaK and is likely to be dominated by electrostatic interactions. J-domain may tether DnaK to DnaJ-bound substrates, which DnaK then binds with its C-terminal peptide-binding domain. The peptide-binding domain of DnaJ is comprised of a β sandwich made up of 6 β-strands divided into 2 sheets.

9 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (9 proteins: gene, accession, name)

• DNAJA1
• DNAJA2
• DNAJA3
• DNAJA4
• DNAJB1
• DNAJB11
• DNAJB13
• DNAJB4
• DNAJB5