Difference between revisions of "ClpE"
Line 91: | Line 91: | ||
=Expression and regulation= | =Expression and regulation= | ||
− | * '''Operon:''' | + | * '''Operon:''' ''clpE'' {{PubMed|10320580}} |
− | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|10320580}} |
− | * '''Regulation:''' induced by heat ([[CtsR]]) [http://www.ncbi.nlm.nih.gov/pubmed | + | * '''Regulation:''' |
− | + | ** induced by heat ([[CtsR]]) [http://www.ncbi.nlm.nih.gov/pubmed/9987115 PubMed] | |
− | * '''Regulatory mechanism:''' [[CtsR]]: transcription repression [http://www.ncbi.nlm.nih.gov/pubmed/9987115 PubMed1], [http://www.ncbi.nlm.nih.gov/pubmed/11179229 PubMed2], [http://www.ncbi.nlm.nih.gov/pubmed/16163393 PubMed3], [http://www.ncbi.nlm.nih.gov/pubmed/17380125 PubMed4 | + | |
− | + | * '''Regulatory mechanism:''' | |
+ | ** [[CtsR]]: transcription repression [http://www.ncbi.nlm.nih.gov/pubmed/9987115 PubMed1], [http://www.ncbi.nlm.nih.gov/pubmed/11179229 PubMed2], [http://www.ncbi.nlm.nih.gov/pubmed/16163393 PubMed3], [http://www.ncbi.nlm.nih.gov/pubmed/17380125 PubMed4] | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Line 123: | Line 124: | ||
=References= | =References= | ||
− | + | <pubmed>10320580 9987115 11179229 16163393 17380125 </pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:52, 3 October 2009
- 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
|
Contents
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
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
Database entries
- Structure:
- UniProt: O31673
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: clpE 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
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)