Difference between revisions of "ClpQ"

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|-
 
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|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
 
|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
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|-
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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]
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|-
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|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]
 
|-
 
|-
 
|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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|-
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13488&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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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 DNA_with_flanks]
 
|-
 
|-
 
|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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|-
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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]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:clpQ_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU16150]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
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<br/><br/>
  
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<br/><br/>
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= [[Categories]] containing this gene/protein =
 +
{{SubtiWiki category|[[proteolysis]]}},
 +
{{SubtiWiki category|[[membrane proteins]]}}
 +
 
 +
= This gene is a member of the following [[regulons]] =
 +
{{SubtiWiki regulon|[[CodY regulon]]}}
  
 
=The gene=
 
=The gene=
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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]
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=== Additional information===
 
=== Additional information===
 +
 +
  
  
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
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* '''Interactions:'''
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* '''[[SubtInteract|Interactions]]:'''
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** [[ClpQ]]-[[ClpY]] {{PubMed|18689473}}
  
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* '''Localization:''' cytoplasm (according to Swiss-Prot)
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* '''[[Localization]]:'''  
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** cytoplasm, forms small foci, usually positioned near the cell membrane, formation of foci depends on the presence of the cognate ATPase [[ClpY]] {{PubMed|18689473}}
  
 
=== 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]
  
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39070 P39070]
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* '''UniProt:''' [http://www.uniprot.org/uniprot/P39070 P39070]
  
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU16150]
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU16150]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
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=Expression and regulation=
 
=Expression and regulation=
  
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* '''Operon:'''  
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* '''Operon:''' ''[[codV]]-[[clpQ]]-[[clpY]]-[[codY]]'' {{PubMed|7783641}}
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpQ_1688114_1688659_1 clpQ] {{PubMed|22383849}}
  
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* '''[[Sigma factor]]:'''  
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* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|7783641}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/11331605 PubMed]
 
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/11331605 PubMed]
  
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* '''Additional information:'''  
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* '''Additional information:'''
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
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==Reviews==
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'''Additional reviews:''' {{PubMed|23479438}}
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==Original publications==
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<pubmed>12805205,11179218,18689473,11331605, 7783641</pubmed>
  
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<pubmed>12805205,11179218,,11331605, </pubmed>
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[[Category:Protein-coding genes]]

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
ClpQ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ClpQ expression.png















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

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)

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