Difference between revisions of "ClpQ"
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU16150 clpQ] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU16150 clpQ] | ||
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| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=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 | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[codV]]'', ''[[clpY]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[codV]]'', ''[[clpY]]'' | ||
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| − | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU16150 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU16150 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU16150 | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU16150 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU16150 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU16150 DNA_with_flanks] |
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|colspan="2" | '''Genetic context''' <br/> [[Image:clpQ_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:clpQ_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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| − | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpQ_1688114_1688659_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:clpQ_expression.png|500px]] | + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpQ_1688114_1688659_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:clpQ_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU16150]] |
|- | |- | ||
|} | |} | ||
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU16150&redirect=T BSU16150] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/codV-clpQY-codY.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/codV-clpQY-codY.html] | ||
| Line 94: | Line 95: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU16150&redirect=T BSU16150] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2Z3B 2Z3B] | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2Z3B 2Z3B] | ||
Latest revision as of 13:43, 2 April 2014
- 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
| |
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
- BsubCyc: BSU16150
- 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
- BsubCyc: BSU16150
- 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)
