ClpQ

• Description: two-component ATP-dependent protease
  
  

Gene name	clpQ
Synonyms	hslV, codW
Essential	no
Product	two-component ATP-dependent protease
Function	protein degradation
Gene expression levels in SubtiExpress: clpQ
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU16150

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • ClpQ-ClpY PubMed

• 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

• BsubCyc: BSU16150

• Structure: 2Z3B

• UniProt: P39070

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: codV-clpQ-clpY-codY PubMed

• Expression browser: clpQ PubMed

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • CodY: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Additional reviews: PubMed

Original publications

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)