Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440
The Disordered C-Terminus of the Chaperone DnaK Increases the Competitive Fitness of Pseudomonas putida and Facilitates the Toxicity of GraT.
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"DnaK facilitates the folding through repeated cycles of ATP-dependent binding and release of an unfolded protein [6]."
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"ATP binding and hydrolysis by DnaK NBD allosterically controls the binding of SBD to its substrates—short hydrophobic peptide segments that would normally be buried in the folded structure."
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"Curiously, the current study demonstrates that toxin activity can also be positively affected by a cellular chaperone, as we show that DnaK facilitates the toxicity of GraT in the absence of its cognate antitoxin GraA."
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.
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"The binding and release of substrate protein for folding involves the following ATP hydrolysis-dependent cycle: (i) unfolded luciferase binds initially to DnaJ; (ii) upon interaction with luciferase-DnaJ, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable luciferase-DnaK-DnaJ complex; (iii) GrpE releases ADP from DnaK; and (iv) ATP binding to DnaK triggers the release of substrate protein, thus completing the reaction cycle."
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"Several rounds of ATP-dependent interaction with DnaK and DnaJ are required for fully efficient folding."
Falcon deep research report for dnaK in Pseudomonas putida KT2440