ClpE

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  • Description: ATP-dependent Clp protease-like (class III stress gene)

Gene name clpE
Synonyms ykvH
Essential no
Product ATP-dependent Clp protease-like
Function protein degradation
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 77 kDa, 5.135
Gene length, protein length 2097 bp, 699 aa
Immediate neighbours motA, ykvI
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ClpE context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU13700

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATPase/chaperone
  • Protein family: AAA+ -type ATPase (IPR013093) InterPro (PF07724) PFAM

Extended information on the protein

  • Kinetic information:
  • Domains: AAA-ATPase PFAM
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: expressed after heat shock, localization in cytoplasmic polar clusters, excluded from the nucleoid, colocalization with ClpP Pubmed

ClpE.jpg

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: clpE::spec available from the Hamoen] Lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion: C-terminal YFP and CFP fusions (single copy) available from the Hamoen] Lab
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

Your additional remarks

References

Janine Kirstein, David A Dougan, Ulf Gerth, Michael Hecker, Kürşad Turgay
The tyrosine kinase McsB is a regulated adaptor protein for ClpCP.
EMBO J: 2007, 26(8);2061-70
[PubMed:17380125] [WorldCat.org] [DOI] (P p)

Janine Kirstein, Daniela Zühlke, Ulf Gerth, Kürşad Turgay, Michael Hecker
A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis.
EMBO J: 2005, 24(19);3435-45
[PubMed:16163393] [WorldCat.org] [DOI] (P p)

E Krüger, D Zühlke, E Witt, H Ludwig, M Hecker
Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor.
EMBO J: 2001, 20(4);852-63
[PubMed:11179229] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, K Devine, M Rose, T Msadek
ClpE, a novel type of HSP100 ATPase, is part of the CtsR heat shock regulon of Bacillus subtilis.
Mol Microbiol: 1999, 32(3);581-93
[PubMed:10320580] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, T Msadek
CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria.
Mol Microbiol: 1999, 31(1);117-31
[PubMed:9987115] [WorldCat.org] [DOI] (P p)