dnaK chaperone protein DnaK [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: dnaK
Official Full Name: chaperone protein DnaK
Primary source: ECOCYC:EG10241
Locus tag: b0014
See related: ASAP:ABE-0000052
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK0014; groPAB; groPC; groPF; grpC; grpF; seg
Summary: ATP-regulated binding and release of polypeptide substrates. [More information is available at EcoGene: EG10241]. Hsc56 exhibits specificity toward Hsc62, as Hsc56 does not activate DnaK or Hsc66 ATPase activity . [More information is available at EcoCyc: EG10241].
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Genomic context

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Sequence:: NC_000913.3 (12163..14079)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cas1-Cas2 physically and functionally interacts with DnaK to modulate CRISPR Adaptation.
Title: Cas1-Cas2 physically and functionally interacts with DnaK to modulate CRISPR Adaptation.
In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
Title: In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States.
Conformational equilibria in allosteric control of Hsp70 chaperones.
Title: Conformational equilibria in allosteric control of Hsp70 chaperones.
J-Domain Proteins in Bacteria and Their Viruses.
Title: J-Domain Proteins in Bacteria and Their Viruses.
The authors find that large aggregates or bulky, native-like substrates activate the DnaK-ClpB complex, whereas a smaller, permanently unfolded protein or extended, short peptides fail to stimulate it.
Title: Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.
We identified that molecular chaperone-encoding dnaK, cell division protein-encoding cpoB and repeat protein-encoding rhsC were associated with the cost reduction for pMCR1_1943, which may represent new mechanisms for host bacterial strains to compensate fitness costs imposed by large plasmids and warrant further studies.
Title: Fitness cost of a mcr-1-carrying IncHI2 plasmid.
Plasmid carrying an E. coli chromosomal fragment harboring chaperone protein DnaK capable of encoding truncated N-terminal ATPase domain (244 aa) can suppress Lon Protease mutant phenotypes in copy number dependent manner. Systematic deletion analysis of dnaK reveals that 169 aa peptide is enough for the suppression of Methyl Methanesulfonate sensitivity phenotype of Deltalon mutant.
Title: Suppression of Δlon phenotypes in Escherichia coli by N-terminal DnaK peptides.
While preventing the formation of lethal IpaC aggregates, DnaK promoted the incorporation of IpaC into large and dynamic complexes (LDCs) restricted at the bacterial pole through nucleoid occlusion. Direct and reversible IpaC-DnaK interactions as part of large dynamic complexes (LDCs) drive polarization through nucleoid occlusion. Polar accumulation was associated with DnaKJ-dependent substrate folding.
Title: Protein polarization driven by nucleoid exclusion of DnaK(HSP70)-substrate complexes.
BAH1, an E3 ligase from plant that has a similar zinc finger domain to DnaJ, can perform block the effect of DnaK on sigma(32) in Escherichia coli.
Title: BAH1 an E3 Ligase from Arabidopsis thaliana Stabilizes Heat Shock Factor σ(32) of Escherichia coli by Interacting with DnaK/DnaJ Chaperone Team.
A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.
Title: A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables ADP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP-dependent protein folding chaperone	IDA Inferred from Direct Assay more info	PubMed
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	IBA Inferred from Biological aspect of Ancestor more info
enables protein folding chaperone	IDA Inferred from Direct Assay more info	PubMed
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables sigma factor antagonist activity	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in cellular response to unfolded protein	IDA Inferred from Direct Assay more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	EXP Inferred from Experiment more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone cofactor-dependent protein refolding	IDA Inferred from Direct Assay more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of DNA-templated transcription	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein unfolding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein-containing complex assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in response to heat	IDA Inferred from Direct Assay more info	PubMed
involved_in response to heat	IEP Inferred from Expression Pattern more info	PubMed
involved_in stress response to copper ion	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in inclusion body	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	HDA more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
part_of protein-containing complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: chaperone protein DnaK

NP_414555.1

EC 3.6.4.10

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

12163..14079

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_414555.1 chaperone protein DnaK [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_414555.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A765TD66

Conserved Domains (1) summary

PRK00290
Location:1 → 638

dnaK; molecular chaperone DnaK; Provisional