Difference between revisions of "DesR"

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|style="background:#ABCDEF;" align="center"|'''Function''' || regulation of  cold shock expression of des
 
|style="background:#ABCDEF;" align="center"|'''Function''' || regulation of  cold shock expression of des
 
|-
 
|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/DesR DesR]
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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=BSU19200 desR]
 
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|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_deg.html Fatty acid degradation]'''
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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=DesR DesR]
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|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=desR desR]'''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 22 kDa, 4.885   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 22 kDa, 4.885   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[desK]]'', ''[[yocH]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[desK]]'', ''[[yocH]]''
 
|-
 
|-
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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:CAB13812&#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=BSU19200 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU19200 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU19200 DNA_with_flanks]
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yocG_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yocG_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=desR_2091705_2092304_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:desR_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU19200]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
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<br/><br/><br/><br/>
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<br/><br/><br/><br/><br/><br/>
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<br/><br/><br/><br/>
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<br/><br/><br/><br/>
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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19200&redirect=T BSU19200]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yocFG.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yocFG.html]
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=== Additional information===
 
=== Additional information===
−
 
−
 
−
 
  
 
=The protein=
 
=The protein=
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
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* '''Interactions:''' [[DesK]]-[[DesR]]
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* '''[[SubtInteract|Interactions]]:'''
 +
** [[DesK]]-[[DesR]]
  
−
* '''Localization:''' cell membrane (according to Swiss-Prot)
+
* '''[[Localization]]:''' cell membrane (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19200&redirect=T BSU19200]
  
 
* '''Structure:'''
 
* '''Structure:'''
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* '''Operon:''' ''[[desK]]-[[desR]]'' {{PubMed|11285232}}
 
* '''Operon:''' ''[[desK]]-[[desR]]'' {{PubMed|11285232}}
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 +
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=desR_2091705_2092304_1 desR] {{PubMed|22383849}}
  
 
* '''Sigma factor:'''  
 
* '''Sigma factor:'''  
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=References=
 
=References=
  
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<pubmed>10094672,12399512, 19595746, 11285232, 17087771 12207704</pubmed>
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<pubmed>10094672,12399512, 19595746, 11285232, 17087771 12207704 25406381 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Latest revision as of 07:02, 24 November 2014

  • Description: two-component response regulator, regulation of cold shock expression of des

Gene name desR
Synonyms yocG
Essential no
Product two-component response regulator
Function regulation of cold shock expression of des
Gene expression levels in SubtiExpress: desR
Interactions involving this protein in SubtInteract: DesR
Metabolic function and regulation of this protein in SubtiPathways:
desR
MW, pI 22 kDa, 4.885
Gene length, protein length 597 bp, 199 aa
Immediate neighbours desK, yocH
Sequences Protein DNA DNA_with_flanks
Genetic context
YocG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DesR expression.png















Categories containing this gene/protein

lipid metabolism/ other, transcription factors and their control, cold stress proteins, membrane proteins, phosphoproteins

This gene is a member of the following regulons

The DesR regulon:

The gene

Basic information

  • Locus tag: BSU19200

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcription activation of the des operon when phosphorylated by DesK
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated by DesK on an Asp residue
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • induced by cold shock (18-fold) 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

Felipe Trajtenberg, Daniela Albanesi, Natalia Ruétalo, Horacio Botti, Ariel E Mechaly, Marcos Nieves, Pablo S Aguilar, Larisa Cybulski, Nicole Larrieux, Diego de Mendoza, Alejandro Buschiazzo
Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.
mBio: 2014, 5(6);e02105
[PubMed:25406381] [WorldCat.org] [DOI] (I e)

Sebastián R Najle, María E Inda, Diego de Mendoza, Larisa E Cybulski
Oligomerization of Bacillus subtilis DesR is required for fine tuning regulation of membrane fluidity.
Biochim Biophys Acta: 2009, 1790(10);1238-43
[PubMed:19595746] [WorldCat.org] [DOI] (P p)

Pablo S Aguilar, Diego de Mendoza
Control of fatty acid desaturation: a mechanism conserved from bacteria to humans.
Mol Microbiol: 2006, 62(6);1507-14
[PubMed:17087771] [WorldCat.org] [DOI] (P p)

Carsten L Beckering, Leif Steil, Michael H W Weber, Uwe Völker, Mohamed A Marahiel
Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis.
J Bacteriol: 2002, 184(22);6395-402
[PubMed:12399512] [WorldCat.org] [DOI] (P p)

Larisa E Cybulski, Daniela Albanesi, María C Mansilla, Silvia Altabe, Pablo S Aguilar, Diego de Mendoza
Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase.
Mol Microbiol: 2002, 45(5);1379-88
[PubMed:12207704] [WorldCat.org] [DOI] (P p)

P S Aguilar, A M Hernandez-Arriaga, L E Cybulski, A C Erazo, D de Mendoza
Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis.
EMBO J: 2001, 20(7);1681-91
[PubMed:11285232] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)

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