ClpC
Revision as of 12:41, 18 April 2012 by 134.76.70.252 (talk)
- Description: ATPase subunit of the ATP-dependent ClpC-ClpP protease, involved in competence development, heat shock regulation, motility, sporulation, protein quality control, biofilm formation
Gene name | clpC |
Synonyms | mecB |
Essential | no |
Product | ATPase subunit of the ClpC-ClpP protease |
Function | protein degradation positive regulator of autolysin (LytC and LytD) synthesis |
Interactions involving this protein in SubtInteract: ClpC | |
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
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
proteolysis, sporulation proteins, general stress proteins (controlled by SigB), heat shock proteins
This gene is a member of the following regulons
CtsR regulon, SigB regulon, SigF regulon
The gene
Basic information
- Locus tag: BSU00860
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
- A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed
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:
Database entries
- 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
Kürsad Turgay, Freie Universität Berlin, Germany homepage
Your additional remarks
References
Reviews
Additional reviews: PubMed
Dorte Frees, Kirsi Savijoki, Pekka Varmanen, Hanne Ingmer
Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria.
Mol Microbiol: 2007, 63(5);1285-95
[PubMed:17302811]
[WorldCat.org]
[DOI]
(P p)
Original Publications
Additional publications: PubMed