A0A6S4GTK4 · A0A6S4GTK4_9BACT

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.

136850100150200250300350
TypeIDPosition(s)Description
Binding site156Zn2+ 1 (UniProtKB | ChEBI)
Binding site159Zn2+ 1 (UniProtKB | ChEBI)
Binding site173Zn2+ 2 (UniProtKB | ChEBI)
Binding site176Zn2+ 2 (UniProtKB | ChEBI)
Binding site199Zn2+ 2 (UniProtKB | ChEBI)
Binding site202Zn2+ 2 (UniProtKB | ChEBI)
Binding site213Zn2+ 1 (UniProtKB | ChEBI)
Binding site216Zn2+ 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
      TM7x_03215

Organism names

  • Taxonomic identifier
  • Strain
    • TM7x
  • Taxonomic lineage
    Bacteria > Candidatus Saccharibacteria > Candidatus Saccharimonadia > Candidatus Nanosynbacterales > Candidatus Nanosynbacteraceae > Candidatus Nanosynbacter

Accessions

  • Primary accession
    A0A6S4GTK4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, zinc finger, repeat.

Type
IDPosition(s)Description
Domain5-67J
Domain143-225CR-type
Zinc finger143-225CR-type
Repeat156-163CXXCXGXG motif
Repeat173-180CXXCXGXG motif
Repeat199-206CXXCXGXG motif
Repeat213-220CXXCXGXG 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
    368
  • Mass (Da)
    39,826
  • Last updated
    2020-12-02 v1
  • Checksum
    C70B92A7CC76B3C4
MSKRDYYEVLGVSKSASEDEIKKAFRKLAVKYHPDKEGGDEAKFKEINEAYEVLKDKQKRQRYDQFGHAGVGGASGGGFSGNPFEGFSGFGGQNVHFDFGDGGLGDIFSQFFGGAPGASGGGRQRGRDIETSVTLSFEDAIFGTEKKISLSLEDECEHCHGDGAEPGFGMKTCPTCKGAGQQTRTMNSLFGQIQQAVVCETCHGKGKVPEKECSVCRGKGTTRQNKDITIKIPAGIDDGATIRLRDRGESVPGGSRGDLYVHIRVKAHKKFTREGNIILSEEHISMVDAALGTEIDVETVDGVITMKIPAGTQSGTDFKLSGHGVPDLRSESRGPHIVGIIVDTPTKLTKKQKELLEQFRGAKKRRLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007496
EMBL· GenBank· DDBJ
AJA06614.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp