Difference between revisions of "ClpC"
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==Original Publications== | ==Original Publications== | ||
<pubmed>9987115,8016067,9000055,12923101,10447896,9141693,2113920,16525504,16497325,19226326,8793870,16163393,10809708,14679237,17560370,11684022,12598648,8195092,11722737,11914365,17380125,12028382,18689476,19361434,9890793, 19767395 ,9987115, 11544224, 17981983, 14763982, 18786145, 8016066 19361434 18689473 20070525 </pubmed> | <pubmed>9987115,8016067,9000055,12923101,10447896,9141693,2113920,16525504,16497325,19226326,8793870,16163393,10809708,14679237,17560370,11684022,12598648,8195092,11722737,11914365,17380125,12028382,18689476,19361434,9890793, 19767395 ,9987115, 11544224, 17981983, 14763982, 18786145, 8016066 19361434 18689473 20070525 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:01, 3 February 2010
- Description: ATP-dependent Clp protease, ATPase subunit
Gene name | clpC |
Synonyms | mecB |
Essential | no |
Product | ATP-dependent Clp protease, ATPase subunit |
Function | protein degradation positive regulator of autolysin (LytC and LytD) synthesis |
Metabolic function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 89 kDa, 5.746 |
Gene length, protein length | 2430 bp, 810 aa |
Immediate neighbours | mcsB, radA |
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: BSU00860
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: mecA family (according to Swiss-Prot) clpA/clpB family. ClpC subfamily (according to Swiss-Prot), AAA+ -type ATPase (IPR013093) InterPro (PF07724) PFAM
Targets of ClpC-ClpP-dependent protein degradation
Extended information on the protein
- Kinetic information:
- Domains: AAA-ATPase PFAM
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with ClpP Pubmed; forms foci coincident with nucleoid edges, usually near cell poles PubMed
Database entries
- Structure: 2K77 (N-terminal domain)
- UniProt: P37571
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulation:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion: C-terminal GFP fusions (single copy, also as CFP and YFP variants) 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
Reviews
Noël Molière, Kürşad Turgay
Chaperone-protease systems in regulation and protein quality control in Bacillus subtilis.
Res Microbiol: 2009, 160(9);637-44
[PubMed:19781636]
[WorldCat.org]
[DOI]
(I p)
Janine Kirstein, Noël Molière, David A Dougan, Kürşad Turgay
Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases.
Nat Rev Microbiol: 2009, 7(8);589-99
[PubMed:19609260]
[WorldCat.org]
[DOI]
(I p)
Original Publications