Difference between revisions of "ClpC"
m (→Targets of ClpC-ClpP-dependent protein degradation) |
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=== Additional information=== | === Additional information=== | ||
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2K77 2K77] (N-terminal domain) | + | * '''Structure:''' |
+ | ** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2K77 2K77] (N-terminal domain) | ||
+ | ** [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3PXG 3PXG] (the [[MecA]]-[[ClpC]] complex) {{PubMed|21368759}} | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37571 P37571] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37571 P37571] | ||
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{{PubMed|19609260,19781636}} | {{PubMed|19609260,19781636}} | ||
==Original Publications== | ==Original Publications== | ||
− | <pubmed>9987115,8016067,9000055,12923101,10447896,9141693,2113920,16497325,19226326,8793870,10809708,14679237,17560370,11684022,8195092,11722737,11914365,12028382,18689476,19361434,9890793, 19767395 ,9987115, 11544224, 17981983, 14763982, 8016066 19361434 18689473 20070525 20923420 20852588 </pubmed> | + | <pubmed>9987115,8016067,9000055,12923101,10447896,9141693,2113920,16497325,19226326,8793870,10809708,14679237,17560370,11684022,8195092,11722737,11914365,12028382,18689476,19361434,9890793, 19767395 ,9987115, 11544224, 17981983, 14763982, 8016066 19361434 18689473 20070525 20923420 20852588 21368759</pubmed> |
Additional publications: {{PubMed|18786145,16525504,17380125,16163393,12598648}} | Additional publications: {{PubMed|18786145,16525504,17380125,16163393,12598648}} | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 08:06, 13 April 2011
- Description: ATP-dependent Clp protease, ATPase subunit of the 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 |
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
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
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:
- Interactions:
- 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
- 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
Original Publications
Additional publications: PubMed