Difference between revisions of "ClpC"
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** the protease: [[ClpC]]-[[ClpP]] | ** the protease: [[ClpC]]-[[ClpP]] | ||
** interactions with adaptor proteins of [[ClpC]]-[[ClpP]]: [[YpbH]]-[[ClpC]], [[McsB]]-[[ClpC]], [[MecA]]-[[ClpC]] [http://www.ncbi.nlm.nih.gov/sites/entrez/10447896 PubMed] | ** interactions with adaptor proteins of [[ClpC]]-[[ClpP]]: [[YpbH]]-[[ClpC]], [[McsB]]-[[ClpC]], [[MecA]]-[[ClpC]] [http://www.ncbi.nlm.nih.gov/sites/entrez/10447896 PubMed] | ||
| + | ** [[CtsR]]-[[ClpP]]/[[ClpC]] (degradation of [[CtsR]]) {{PubMed|11179229,16163393,17380125}} | ||
| + | ** [[McsB]]-[[ClpP]]/[[ClpC]] (rapid degradation of non-phosphorylated McsB) {{PubMed|20852588}} | ||
* '''Localization:''' cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with [[ClpP]] [http://www.ncbi.nlm.nih.gov/pubmed/18786145 Pubmed]; forms foci coincident with nucleoid edges, usually near cell poles {{PubMed|18689473}} | * '''Localization:''' cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with [[ClpP]] [http://www.ncbi.nlm.nih.gov/pubmed/18786145 Pubmed]; forms foci coincident with nucleoid edges, usually near cell poles {{PubMed|18689473}} | ||
| Line 135: | Line 137: | ||
{{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 </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 </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 08:55, 26 October 2010
- Description: ATP-dependent Clp protease, ATPase subunit of the ClpC-ClpP protease, involved in auto-cleavage of SlrR
| 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
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
- 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
Original Publications
Additional publications: PubMed
