A0A0T9NT44 · A0A0T9NT44_9GAMM

  • Protein
    Chaperone protein DnaJ
  • Gene
    dnaJ
  • Status
    UniProtKB unreviewed (TrEMBL)
  • 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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per monomer.

Features

Showing features for binding site.

137650100150200250300350
TypeIDPosition(s)Description
Binding site144Zn2+ 1 (UniProtKB | ChEBI)
Binding site147Zn2+ 1 (UniProtKB | ChEBI)
Binding site161Zn2+ 2 (UniProtKB | ChEBI)
Binding site164Zn2+ 2 (UniProtKB | ChEBI)
Binding site183Zn2+ 2 (UniProtKB | ChEBI)
Binding site186Zn2+ 2 (UniProtKB | ChEBI)
Binding site197Zn2+ 1 (UniProtKB | ChEBI)
Binding site200Zn2+ 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
    • ORF names
      HB980_09540

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SCPM-O-B-8025
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Yersinia

Accessions

  • Primary accession
    A0A0T9NT44

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat144-151CXXCXGXG motif
Repeat161-168CXXCXGXG motif
Repeat183-190CXXCXGXG motif
Repeat197-204CXXCXGXG 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
    376
  • Mass (Da)
    40,961
  • Last updated
    2016-02-17 v1
  • MD5 Checksum
    90D72FCB9715D66E7CADD021E45DC904
MAKRDYYEVLGVKKDADEREIKKAYKRLAVKYHPDRNQDENDTGENFKEVKEAYEILTDPQKRAAYDQYGHAAFEQGGMGGGGFGGGGADFSDIFGDVFGDIFGGGRRQRASRGSDLRYNMDLTLEEAVRGVTKEIRIPTLNECDVCHGSGAKPGSSPVTCSTCRGAGQVHMRQGFFTVQQACPTCHGSGQIIKDPCNKCHGHGRVEKSKTLSVKIPAGVDTGDRIRLSGEGEAGEHGAPAGDLYVQVQVKAHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPAETQTGKLFRMRGKGVKSVRGGSQGDLLCRVVVETPVHLSEKQKQLLRELEESFVGAAGEKNSPRSKSFLDGVKKFFDDLTR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAASAN010000003
EMBL· GenBank· DDBJ
NIL26790.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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