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Overview
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Pathways & interactions
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Cross-references
HSP40/DnaJ peptide-binding (IPR008971)
Short name: HSP40/DnaJ_pept-bd
Overlapping entries
- Chaperone DnaJ, C-terminal (IPR002939)
- Chaperone DnaJ (IPR012724)
- DNA-binding protein, curved-DNA (IPR023859)
Description
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
- SSF49493 (SSF49493)