P48207 · DNAJ_FRATU

  • Protein
    Chaperone protein DnaJ
  • Gene
    dnaJ
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

137150100150200250300350
TypeIDPosition(s)Description
Binding site140Zn2+ 1 (UniProtKB | ChEBI)
Binding site143Zn2+ 1 (UniProtKB | ChEBI)
Binding site156Zn2+ 2 (UniProtKB | ChEBI)
Binding site159Zn2+ 2 (UniProtKB | ChEBI)
Binding site178Zn2+ 2 (UniProtKB | ChEBI)
Binding site181Zn2+ 2 (UniProtKB | ChEBI)
Binding site192Zn2+ 1 (UniProtKB | ChEBI)
Binding site195Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Thiotrichales > Francisellaceae > Francisella

Accessions

  • Primary accession
    P48207

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000707861-371Chaperone protein DnaJ

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Features

Showing features for domain, zinc finger, repeat.

TypeIDPosition(s)Description
Domain5-70J
Zinc finger127-204CR-type
Repeat140-147CXXCXGXG motif
Repeat156-163CXXCXGXG motif
Repeat178-185CXXCXGXG motif
Repeat192-199CXXCXGXG 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    371
  • Mass (Da)
    41,481
  • Last updated
    1996-02-01 v1
  • Checksum
    BBDC7F3B4741EF1E
MQQKCYYEILNISKTASGVEIKRAYRKLAMKYHPDRNPGDKEAEIKFKEISEAYEILSDDSKRSRYDQFGHAGVNQQSGFGGTGGFEDIFDTFFGGGTSRGSNRSRASRGSDLEYTLEITLEEAFFGVEKEITIPRMESCDSCDGTGSKSRSKTTCHACHGQGTIRRQQGFFAFEQTCPVCNGTGYSITDPCDACYGNGKVKKQKTLKVKIPEGVDNGDRIRLQGEGDSGSNGAMNGDLYVQIIIKEHKIFERRDINLYCEMPISFTKACLGGDIKVPTLDGEVVLKVVPETQTGKVFRLREKGMKSLRGHRRGDLLCKVVVETPVNLSAEQKELLEKFADSLGEDYQSKHAPKSKTWFDNVKDYAKKFFE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L43367
EMBL· GenBank· DDBJ
AAA69562.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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