Difference between revisions of "ClpC"

From SubtiWiki
Jump to: navigation, search
(Categories containing this gene/protein)
Line 93: Line 93:
  
 
* '''Modification:'''
 
* '''Modification:'''
 +
** phosphorylated on Arg-5 and Arg-254 {{PubMed|22517742}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
Line 169: Line 170:
 
==Original Publications==
 
==Original Publications==
 
'''Additional publications:''' {{PubMed|18786145,16525504,17380125,16163393,12598648}}
 
'''Additional publications:''' {{PubMed|18786145,16525504,17380125,16163393,12598648}}
<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   21622759 21368759 21821766</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 22517742  21622759 21368759 21821766</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:21, 21 April 2012

  • 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
ClpC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ClpC expression.png




























Categories containing this gene/protein

proteolysis, sporulation proteins, general stress proteins (controlled by SigB), heat shock proteins, phosphoproteins

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:
    • phosphorylated on Arg-5 and Arg-254 PubMed
  • 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

  • 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

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