ClpE

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU13700

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Categories containing this gene/protein

proteolysis, heat shock proteins

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATPase/chaperone

• Protein family: AAA+ -type ATPase (IPR013093) InterPro (PF07724) PFAM

• Paralogous protein(s): ClpC, ClpX

Extended information on the protein

• Kinetic information:

• Domains: AAA-ATPase PFAM

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: ClpE-ClpP

• Localization: localization in cytoplasmic polar clusters, excluded from the nucleoid, colocalization with ClpP Pubmed; forms foci coincident with nucleoid edges, usually near cell poles PubMed

Database entries

• Structure:

• UniProt: O31673

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: clpE PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by heat (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

• 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

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)