Difference between revisions of "ClpC"
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| − | * '''Description:''' ATP-dependent Clp protease, ATPase subunit <br/><br/> | + | * '''Description:''' ATP-dependent Clp protease, ATPase subunit of the [[ClpC]]-[[ClpP]] protease<br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || ATPase subunit of the [[ClpC]]-[[ClpP]] protease |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation<br/>positive regulator of autolysin ([[LytC]] and [[LytD]]) synthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation<br/>positive regulator of autolysin ([[LytC]] and [[LytD]]) synthesis | ||
| Line 61: | Line 61: | ||
=== Targets of [[ClpC]]-[[ClpP]]-dependent protein degradation === | === Targets of [[ClpC]]-[[ClpP]]-dependent protein degradation === | ||
| − | * [[DegU]]-P {{PubMed|20070525}} | + | * [[DegU]]-P {{PubMed|20070525}}, [[ComK]], [[Mdh]] |
=== Extended information on the protein === | === Extended information on the protein === | ||
| Line 75: | Line 75: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' [[YpbH]]-[[ClpC]], [[McsB]]-[[ClpC]], [[ | + | * '''Interactions:''' |
| + | ** 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] | ||
* '''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}} | ||
Revision as of 18:04, 20 June 2010
| 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
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
