Difference between revisions of "ClpQ"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[proteolysis]]}}, | ||
| + | {{SubtiWiki category|[[membrane proteins]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
| + | {{SubtiWiki regulon|[[CodY regulon]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 19:38, 8 December 2010
- Description: two-component ATP-dependent protease
| Gene name | clpQ |
| Synonyms | hslV, codW |
| Essential | no |
| Product | two-component ATP-dependent protease |
| Function | protein degradation |
| 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 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
proteolysis, membrane proteins
This gene is a member of the following regulons
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
- Structure: 2Z3B
- UniProt: P39070
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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)
