Difference between revisions of "DesK"

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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/DesK DesK]
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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=BSU19190 desK]
 
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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=DesK DesK]
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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=desK desK]'''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 42 kDa, 9.428   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 42 kDa, 9.428   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[des]]'', ''[[desR]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[des]]'', ''[[desR]]''
 
|-
 
|-
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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:CAB13811&#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=BSU19190 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU19190 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU19190 DNA_with_flanks]
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yocF_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yocF_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=desK_2090574_2091686_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:desK_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU19190]]
 
|-
 
|-
 
|}
 
|}
  
 
__TOC__
 
__TOC__
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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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* '''Locus tag:''' BSU19190
 
* '''Locus tag:''' BSU19190
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−
[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=desK_2090574_2091686_1 Expression]
 
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19190&redirect=T BSU19190]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yocFG.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yocFG.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU19190&redirect=T BSU19190]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3EHF 3EHF]
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3EHF 3EHF]
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* '''Operon:''' ''[[desK]]-[[desR]]'' {{PubMed|11285232}}
 
* '''Operon:''' ''[[desK]]-[[desR]]'' {{PubMed|11285232}}
  
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* '''Sigma factor:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=desK_2090574_2091686_1 desK] {{PubMed|22383849}}
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
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<pubmed> 20117042, 17087771</pubmed>
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<pubmed> 20117042, 17087771 24819366 </pubmed>
 +
 
 
==Original publications==
 
==Original publications==
−
<pubmed>10094672,14734164,12399512,20507988 , 19233289 11285232 19805278 15090506, 12207704 20705470 </pubmed>
+
<pubmed>10094672,14734164,12399512,20507988 , 19233289 11285232 19805278 15090506, 12207704 20705470 23356219 24574048 24522108 25406381 26172072 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Latest revision as of 09:21, 15 July 2015

  • Description: two-component sensor kinase, regulation of cold shock expression of des

Gene name desK
Synonyms yocF
Essential no
Product two-component sensor kinase
Function regulation of cold shock expression of des
Gene expression levels in SubtiExpress: desK
Interactions involving this protein in SubtInteract: DesK
Metabolic function and regulation of this protein in SubtiPathways:
desK
MW, pI 42 kDa, 9.428
Gene length, protein length 1110 bp, 370 aa
Immediate neighbours des, desR
Sequences Protein DNA DNA_with_flanks
Genetic context
YocF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DesK expression.png















Categories containing this gene/protein

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

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU19190

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of DesR
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • 5 transmembrane helices
    • cytoplasmatic C-terminal trail
  • Modification: autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity: unsaturated fatty acids are negative effectors of the system

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

  • DesK has the ability to sense changes in membrane fluidity PubMed

Expression and regulation

  • Regulation:
    • induced by cold shock (12-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

Reviews


Original publications

Emilio Saita, Luciano A Abriata, Yi Ting Tsai, Felipe Trajtenberg, Thomas Lemmin, Alejandro Buschiazzo, Matteo Dal Peraro, Diego de Mendoza, Daniela Albanesi
A coiled coil switch mediates cold sensing by the thermosensory protein DesK.
Mol Microbiol: 2015, 98(2);258-71
[PubMed:26172072] [WorldCat.org] [DOI] (I p)

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)

Lucía Porrini, Larisa E Cybulski, Silvia G Altabe, María C Mansilla, Diego de Mendoza
Cerulenin inhibits unsaturated fatty acids synthesis in Bacillus subtilis by modifying the input signal of DesK thermosensor.
Microbiologyopen: 2014, 3(2);213-24
[PubMed:24574048] [WorldCat.org] [DOI] (I p)

María Eugenia Inda, Michel Vandenbranden, Ariel Fernández, Diego de Mendoza, Jean-Marie Ruysschaert, Larisa Estefanía Cybulski
A lipid-mediated conformational switch modulates the thermosensing activity of DesK.
Proc Natl Acad Sci U S A: 2014, 111(9);3579-84
[PubMed:24522108] [WorldCat.org] [DOI] (I p)

Mariana Martín, Diego de Mendoza
Regulation of Bacillus subtilis DesK thermosensor by lipids.
Biochem J: 2013, 451(2);269-75
[PubMed:23356219] [WorldCat.org] [DOI] (I p)

Larisa E Cybulski, Mariana Martín, María C Mansilla, Ariel Fernández, Diego de Mendoza
Membrane thickness cue for cold sensing in a bacterium.
Curr Biol: 2010, 20(17);1539-44
[PubMed:20705470] [WorldCat.org] [DOI] (I p)

Felipe Trajtenberg, Martin Graña, Natalia Ruétalo, Horacio Botti, Alejandro Buschiazzo
Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase.
J Biol Chem: 2010, 285(32);24892-903
[PubMed:20507988] [WorldCat.org] [DOI] (I p)

Daniela Albanesi, Mariana Martín, Felipe Trajtenberg, María C Mansilla, Ahmed Haouz, Pedro M Alzari, Diego de Mendoza, Alejandro Buschiazzo
Structural plasticity and catalysis regulation of a thermosensor histidine kinase.
Proc Natl Acad Sci U S A: 2009, 106(38);16185-90
[PubMed:19805278] [WorldCat.org] [DOI] (I p)

Mariana Martín, Daniela Albanesi, Pedro M Alzari, Diego de Mendoza
Functional in vitro assembly of the integral membrane bacterial thermosensor DesK.
Protein Expr Purif: 2009, 66(1);39-45
[PubMed:19233289] [WorldCat.org] [DOI] (I p)

Daniela Albanesi, María Cecilia Mansilla, Diego de Mendoza
The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator.
J Bacteriol: 2004, 186(9);2655-63
[PubMed:15090506] [WorldCat.org] [DOI] (P p)

Karen Hunger, Carsten L Beckering, Mohamed A Marahiel
Genetic evidence for the temperature-sensing ability of the membrane domain of the Bacillus subtilis histidine kinase DesK.
FEMS Microbiol Lett: 2004, 230(1);41-6
[PubMed:14734164] [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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