O85213 · DNAJ_CAMJE

Function

function

Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per monomer.

Features

Showing features for binding site.

137350100150200250300350
TypeIDPosition(s)Description
Binding site148Zn2+ 1 (UniProtKB | ChEBI)
Binding site151Zn2+ 1 (UniProtKB | ChEBI)
Binding site164Zn2+ 2 (UniProtKB | ChEBI)
Binding site167Zn2+ 2 (UniProtKB | ChEBI)
Binding site186Zn2+ 2 (UniProtKB | ChEBI)
Binding site189Zn2+ 2 (UniProtKB | ChEBI)
Binding site200Zn2+ 1 (UniProtKB | ChEBI)
Binding site203Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionheat shock protein binding
Molecular Functionunfolded protein binding
Molecular Functionzinc ion binding
Biological Processchaperone cofactor-dependent protein refolding
Biological ProcessDNA replication
Biological Processprotein refolding
Biological Processresponse to heat

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chaperone protein DnaJ

Gene names

    • Name
      dnaJ
    • Ordered locus names
      Cj1260c

Organism names

Accessions

  • Primary accession
    O85213
  • Secondary accessions
    • O68797
    • Q0P8Z6
    • Q9PN37

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000707511-373Chaperone protein DnaJ

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, zinc finger, repeat.

TypeIDPosition(s)Description
Domain4-69J
Zinc finger135-212CR-type
Repeat148-155CXXCXGXG motif
Repeat164-171CXXCXGXG motif
Repeat186-193CXXCXGXG motif
Repeat200-207CXXCXGXG motif

Domain

The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.

Sequence similarities

Belongs to the DnaJ family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    373
  • Mass (Da)
    41,523
  • Last updated
    2000-12-01 v2
  • Checksum
    653F46CBF489D2CD
MEISYYEILEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSSSSGFGGFEDLGDIFSSFFGEGFGSSRRRKSSNDEKIPSDFIVNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGIGEKASEKCSDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRMGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKITNWFKS

Sequence caution

The sequence AAC08023.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict57in Ref. 2; AAC08023
Sequence conflict71-72in Ref. 1; AAC32328
Sequence conflict86in Ref. 2; AAC08023
Sequence conflict211in Ref. 2; AAC08023
Sequence conflict320in Ref. 2; AAC08023
Sequence conflict334in Ref. 2; AAC08023
Sequence conflict359in Ref. 2; AAC08023
Sequence conflict368in Ref. 2; AAC08023

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF052661
EMBL· GenBank· DDBJ
AAC32328.1
EMBL· GenBank· DDBJ
Genomic DNA
AF053962
EMBL· GenBank· DDBJ
AAC08023.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift
AL111168
EMBL· GenBank· DDBJ
CAL35375.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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