Difference between revisions of "ClpQ"
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpQ_1688114_1688659_1 clpQ] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpQ_1688114_1688659_1 clpQ] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigA]] {{PubMed|7783641}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|7783641}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
− | + | ==Reviews== | |
+ | '''Additional reviews:''' {{PubMed|23479438}} | ||
+ | ==Original publications== | ||
<pubmed>12805205,11179218,18689473,11331605, 7783641</pubmed> | <pubmed>12805205,11179218,18689473,11331605, 7783641</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:36, 14 March 2013
- 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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
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:
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
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)