DesK

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

The gene

Basic information

• Locus tag: BSU19190

Database entries

• BsubCyc: BSU19190

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Interactions:
  • DesK-DesR

• Localization: membrane (transmembrane segments)

Database entries

• BsubCyc: BSU19190

• Structure: 3EHF

• UniProt: O34757

• KEGG entry: [3]

• E.C. number:

Additional information

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

Expression and regulation

• Operon: desK-desR PubMed

• Expression browser: desK PubMed

• Sigma factor:

• 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

• Diego de Mendoza, Universidad Nacional de Rosario, Argentine homepage
• Mohamed Marahiel, Marburg University, Germany homepage

References

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)