A0A2T0RJM3 · A0A2T0RJM3_9BACT

  • 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.

138750100150200250300350
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
      CLV58_15112

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 28354
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Cytophagaceae > Spirosoma

Accessions

  • Primary accession
    A0A2T0RJM3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, zinc finger, repeat.

TypeIDPosition(s)Description
Domain6-71J
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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    387
  • Mass (Da)
    41,807
  • Last updated
    2018-07-18 v1
  • Checksum
    D1D6150F33C3ECCC
MATKRDYYEVLGVDKGVSADDLKKAYRKMAIKYHPDKNPDDPTAEEKFKEAAEAYDVLNDPQKKARYDQFGHAGMGGAAGGGYGAGGPSMDDIFSQFGDVFGDDSPFGSFFRGGQGGGQRQRVRRGSDLRIKLKLNLQEVANGVEKKIKVKRHVTCTTCGGNGSKNGTAVQTCSTCSGTGQTRKVVNTMLGQMVSTSTCPTCNGEGKLVTDRCDVCFGEGRVLQEDVIPLKIPAGVAEGIQLSVGGKGNVPPRGGVAGDLLIVVEEEEDPDLKRDGNNVVFDLYVNFVDAAIGTSVEVPTIDGKARITLEPGTQSGRILRLKGKGIKELNGYGRGDELVHVNVWTPKSLSSEERNMLEKLRNSPNFQPKPNKNEKGFFDKMKDFFHG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PVTE01000051
EMBL· GenBank· DDBJ
PRY21385.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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