DnaK

• Description: class I heat-shock protein (molecular chaperone)
  
  

Gene name	dnaK
Synonyms
Essential	no
Product	class I heat-shock protein (molecular chaperone)
Function	protein quality control
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	65 kDa, 4.571
Gene length, protein length	1833 bp, 611 aa
Immediate neighbours	surC, grpE
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU25470

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: heat shock protein 70 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions: DnaK-DnaJ

• Localization: cytoplasm (according to Swiss-Prot), Membrane-proximal (Spotty) PubMed

Database entries

• Structure:

• UniProt: P17820

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hrcA-grpE-dnaK-dnaJ-yqeT-yqeU-yqeV PubMed

• Sigma factor: SigA PubMed

• Regulation: induced by heat shock (HrcA) PubMed

• Regulatory mechanism: repressed at normal temperature by HrcA

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Wolfgang Schumann, Bayreuth University, Germany Homepage

References

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Dindo Y Reyes, Hirofumi Yoshikawa
DnaK chaperone machine and trigger factor are only partially required for normal growth of Bacillus subtilis.
Biosci Biotechnol Biochem: 2002, 66(7);1583-6
[PubMed:12224648] [WorldCat.org] [DOI] (P p)

G Homuth, A Mogk, W Schumann
Post-transcriptional regulation of the Bacillus subtilis dnaK operon.
Mol Microbiol: 1999, 32(6);1183-97
[PubMed:10383760] [WorldCat.org] [DOI] (P p)

G Homuth, S Masuda, A Mogk, Y Kobayashi, W Schumann
The dnaK operon of Bacillus subtilis is heptacistronic.
J Bacteriol: 1997, 179(4);1153-64
[PubMed:9023197] [WorldCat.org] [DOI] (P p)

A Schulz, B Tzschaschel, W Schumann
Isolation and analysis of mutants of the dnaK operon of Bacillus subtilis.
Mol Microbiol: 1995, 15(3);421-9
[PubMed:7540247] [WorldCat.org] [DOI] (P p)

M Wetzstein, U Völker, J Dedio, S Löbau, U Zuber, M Schiesswohl, C Herget, M Hecker, W Schumann
Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis.
J Bacteriol: 1992, 174(10);3300-10
[PubMed:1339421] [WorldCat.org] [DOI] (P p)