NP_414556.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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Molecular Weight
41,100 Da
NCBI Official Full Name
chaperone Hsp40, DnaK co-chaperone
NCBI Official Synonym Symbols
ECK0015; faa; groP; grpC; JW0014 [Similar Products]
NCBI Protein Information
chaperone Hsp40, DnaK co-chaperone
UniProt Protein Name
Chaperone protein DnaJ
UniProt Synonym Protein Names
HSP40; Heat shock protein J
UniProt Synonym Gene Names
UniProt Entry Name
DNAJ_ECOLI
NCBI Summary for DnaJ
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].
UniProt Comments for DnaJ
Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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.
Research Articles on DnaJ
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