Homologous Superfamily

HSP40/DnaJ peptide-binding (IPR008971)

Short name: HSP40/DnaJ_pept-bd

Overlapping entries


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 beta sandwich made up of 6 beta-strands divided into 2 sheets.

GO terms

Biological Process

GO:0006457 protein folding

Molecular Function

GO:0051082 unfolded protein binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.