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    dnaJ chaperone protein DnaJ [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944753, updated on 19-Sep-2024

    Summary

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    Official Symbol
    dnaJ
    Official Full Name
    chaperone protein DnaJ
    Primary source
    ECOCYC:EG10240
    Locus tag
    b0015
    See related
    ASAP:ABE-0000054
    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
    ECK0015; groP; grpC
    Summary
    DnaK and DnaJ both bind to the same target peptide, forming a ternary complex. [More information is available at EcoGene: EG10240]. The DnaK system of Escherichia coli is a homolog of the eukaryotic Hsp70 chaperone system. [More information is available at EcoCyc: EG10240].
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    Genomic context

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    Sequence:
    NC_000913.3 (14168..15298)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF2541 domain-containing protein YaaI Neighboring gene chaperone protein DnaK Neighboring gene IS186/IS421 family transposase Neighboring gene protein HokC Neighboring gene regulatory protein MokC

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Genetic and biochemical characterization of mutations affecting the carboxy-terminal domain of the Escherichia coli molecular chaperone DnaJ. Goffin L, et al. Mol Microbiol, 1998 Oct. PMID 9791178
    2. Increased persistence in Escherichia coli caused by controlled expression of toxins or other unrelated proteins. Vázquez-Laslop N, et al. J Bacteriol, 2006 May. PMID 16672603, Free PMC Article
    3. The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity: a small angle X-ray scattering study in solution. Shi YY, et al. J Biol Chem, 2005 Jun 17. PMID 15849180
    4. Contributions of cysteine residues in Zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ. Shi YY, et al. Biochemistry, 2005 Feb 8. PMID 15683252
    5. The roles of the two zinc binding sites in DnaJ. Linke K, et al. J Biol Chem, 2003 Nov 7. PMID 12941935

    See all (159) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. Potentiation of the activity of Escherichia coli chaperone DnaJ by tailing hyper-acidic minipeptides.
      Title: Potentiation of the activity of Escherichia coli chaperone DnaJ by tailing hyper-acidic minipeptides.
    3. BAH1 could partially compensate for the DnaJ' zinc finger domain in vivo, and that it was dependent on the zinc finger domain of BAH1.
      Title: BAH1 an E3 Ligase from Arabidopsis thaliana Stabilizes Heat Shock Factor σ(32) of Escherichia coli by Interacting with DnaK/DnaJ Chaperone Team.
    4. These results suggest that, in the absence of interaction with Escherichia coli DnaJ, the N-terminal domain of the MS2 bacteriophage L lysis protein interferes with its ability to bind to its unknown target.
      Title: MS2 Lysis of Escherichia coli Depends on Host Chaperone DnaJ.
    5. Fatty acid methyl esters analysis indicated that the amount of unsaturated fatty acid sharply increased and subcellular location prediction analysis showed a marked decrease in transcription of inner-membrane protein genes, which might have triggered the development of aberrant cell shape and susceptibility for some antibiotics in the DeltadnaKJ strain.
      Title: Large-scale gene expression profiling reveals physiological response to deletion of chaperone dnaKJ in Escherichia coli.
    6. The interaction of DnaK with DnaJ, GrpE, or sigma32 becomes weaker when DnaK is glutathionylated during oxidative stress, and the interaction is restored upon deglutathionylation.
      Title: Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.
    7. analysis of DnaJ-DnaK-GrpE chaperone cooperation
      Title: Action of the Hsp70 chaperone system observed with single proteins.
    8. DnaJ mutant is impaired in biofilm development when exposed to 42 degrees C for 2 h.
      Title: Chaperone DnaJ Influences the Formation of Biofilm by Escherichia coli.
    9. DnaJ-promoted binding of DnaK to multiple sites on sigma32 in the presence of ATP.
      Title: DnaJ-promoted binding of DnaK to multiple sites on σ32 in the presence of ATP.
    10. Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB
      Title: [Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB].
    Submit: New GeneRIF Correction See all GeneRIFs (31)

    Pathways from PubChem

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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

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heat shock protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein disulfide isomerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein-disulfide reductase activity 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 IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within DNA replication IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in chaperone cofactor-dependent protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within chaperone cofactor-dependent protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in chaperone cofactor-dependent protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in negative regulation of DNA-templated transcription IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within 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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within response to heat IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within response to heat IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within viral process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within viral process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    chaperone protein DnaJ

    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

    1. NC_000913.3 Reference assembly

      Range
      14168..15298
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414556.1 chaperone protein DnaJ [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414556.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376MCT3
      Conserved Domains (1) summary
      PRK10767
      Location:1 → 372
      PRK10767; chaperone protein DnaJ; Provisional
    Nucleotide Protein
    Heading Accession and Version

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