Difference between revisions of "ClpC"

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(The protein)
(Reviews)
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==Reviews==
 
==Reviews==
<pubmed> 19609260 </pubmed>
+
<pubmed> 19609260 19781636 </pubmed>
 +
 
 
==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
ClpC context.gif
This image was kindly provided by SubtiList







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

ClpC.jpg

Database entries

  • Structure: 2K77 (N-terminal domain)
  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and 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