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ProteomicsTyrosine 601 of Bacillus subtilis DnaK undergoes phosphorylation and is crucial for chaperone activity and heat shock survival
In order to screen for cellular substrates of the Bacillus subtilis BY-kinase PtkA, and its cognate phosphotyrosine-protein phosphatase PtpZ, we performed a triple SILAC-based quantitative phosphoproteome analysis. Detected tyrosine phosphorylation sites for which the phosphorylation level decreased...
ORGANISM(S): Bacillus subtilis 
2016-05-09 | PXD003764 | Pride
Molecular chaperons Silac Protein phosphorylation Quantitative phosphoproteomics Bacterial protein-tyrosine kinases Protein folding 
ProteomicsCas1-Cas2 and DnaK physically and functionally interact to modulate CRISPR Adaptation
Prokaryotic Cas1-Cas2 protein complexes generate adaptive immunity to mobile genetic elements (MGEs), by capture and integration of MGE DNA in to CRISPR sites. De novo immunity relies on Cas1-Cas2 targeting MGE DNA, without the aid of pre-existing immunity complexes, through mechanisms of ‘naive ada...
ORGANISM(S): Escherichia coli 
2023-05-18 | PXD042090 | Pride
Crispr Cas1-cas2 Adaptaion Dnak 
Proteomicsproteomic analysis of dnaK deletion in Cronobacter sakazakii BAA-894
The protein profiles of both the dnaK deletion mutant and the wild-type strain were analyzed using proteomic analysis. The dnaK deletion mutant was analyzed three times and the wild-type strain was also analyzed three times.
ORGANISM(S): Cronobacter Sakazakii 
2023-02-16 | PXD040215 |
GenomicsGene expression profiling of catfish after treatment with Flavobacterium columnare DnaK protein
Gene expression profiling of catfish after treatment with Flavobacterium columnare DnaK protein
PRJNA495754 | ENA
ProteomicsCharacterization of the interactome profiling of Mycoplasma DnaK in cancer cell reveals interference with key cellular pathways
Chaperone proteins are redundant in nature and, to achieve their function, they bind a large repertoire of client proteins. DnaK is a bacterial chaperone protein that recognizes misfolded and aggregated proteins and drives their folding and intracellular trafficking. Some Mycoplasmas are associated ...
ORGANISM(S): Homo sapiens (Human) 
2022-10-12 | PXD035477 | Pride
Proteomics Cellular pathways Chaperone protein Dnak protein Mycoplasma fermentans 
ProteomicsDnaK interaction and folding of firefly luciferase studied by hydrogen/deuterium exchange – mass spectrometry
The ATP-dependent chaperones of the Hsp70 class (DnaK in E. coli) function in protein folding in cooperation with J proteins and nucleotide exchange factors (DnaJ and GrpE in E. coli, respectively). Hsp70 prevents protein aggregation, increasing the folding yield, but whether it also enhances the ra...
ORGANISM(S): Escherichia coli 
2020-01-15 | PXD016509 | Pride
Deuterium exchange Chaperone Firefly luciferase Dnak Folding 
ProteomicsDual effect of Staphylococcus epidermidis DnaK on Staphylococcus aureus biofilm proteostasis and regulation
Staphylococcus aureus and Staphylococcus epidermidis, two Gram-positive bacteria commonly found in the human skin microbiota, form biofilms that contribute to skin dysbiosis and play a key role in conditions like acne and atopic dermatitis. The Calcitonin Gene-Related Peptide (CGRP) is a human pepti...
ORGANISM(S): Staphylococcus aureus 
2026-03-09 | PXD062742 | Pride
Dnak  biofilm  staphylococcus epidermidis  staphylococcus aureus  skin microbiota 
GenomicsStaphylococcus epidermidis DnaK chaperone protein inhibits Staphylococcus aureus CIP 107093 biofilm formation and induces an accumulation of the exfoliative toxin A
Staphylococcus epidermidis DnaK chaperone protein inhibits Staphylococcus aureus CIP 107093 biofilm formation and induces an accumulation of the exfoliative toxin A
PRJEB85076 | ENA
UnknownAn essential nonredundant role for mycobacterial DnaK in native protein folding.
Not available
S-EPMC4109909 | biostudies-literature
UnknownHsp90, DnaK, and ClpB collaborate in protein reactivation.
Not available
S-EPMC11804706 | biostudies-literature
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