Difference between revisions of "ClpQ"

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|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
 
|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/ClpQ ClpQ]
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 6.105   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 19 kDa, 6.105   

Revision as of 18:02, 30 July 2011

  • Description: two-component ATP-dependent protease

Gene name clpQ
Synonyms hslV, codW
Essential no
Product two-component ATP-dependent protease
Function protein degradation
Interactions involving this protein in SubtInteract: ClpQ
MW, pI 19 kDa, 6.105
Gene length, protein length 543 bp, 181 aa
Immediate neighbours codV, clpY
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ClpQ context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

proteolysis, membrane proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

  • Locus tag: BSU16150

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: HslV subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm, forms small foci, usually positioned near the cell membrane, formation of foci depends on the presence of the cognate ATPase ClpY PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Lyle A Simmons, Alan D Grossman, Graham C Walker
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
J Bacteriol: 2008, 190(20);6758-68
[PubMed:18689473] [WorldCat.org] [DOI] (I p)

Min Suk Kang, Soon Rae Kim, Pyeongsu Kwack, Byung Kook Lim, Sung Won Ahn, Young Min Rho, Ihn Sik Seong, Seong-Chul Park, Soo Hyun Eom, Gang-Won Cheong, Chin Ha Chung
Molecular architecture of the ATP-dependent CodWX protease having an N-terminal serine active site.
EMBO J: 2003, 22(12);2893-902
[PubMed:12805205] [WorldCat.org] [DOI] (P p)

M Ratnayake-Lecamwasam, P Serror, K W Wong, A L Sonenshein
Bacillus subtilis CodY represses early-stationary-phase genes by sensing GTP levels.
Genes Dev: 2001, 15(9);1093-103
[PubMed:11331605] [WorldCat.org] [DOI] (P p)

M S Kang, B K Lim, I S Seong, J H Seol, N Tanahashi, K Tanaka, C H Chung
The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine protease.
EMBO J: 2001, 20(4);734-42
[PubMed:11179218] [WorldCat.org] [DOI] (P p)

F J Slack, P Serror, E Joyce, A L Sonenshein
A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon.
Mol Microbiol: 1995, 15(4);689-702
[PubMed:7783641] [WorldCat.org] [DOI] (P p)