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

• 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

• 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

Reviews

Richard C Stewart
Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.
Curr Opin Microbiol: 2010, 13(2);133-41
[PubMed:20117042] [WorldCat.org] [DOI] (I 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)

Original publications

Michael Kohlstedt, Praveen K Sappa, Hanna Meyer, Sandra Maaß, Adrienne Zaprasis, Tamara Hoffmann, Judith Becker, Leif Steil, Michael Hecker, Jan Maarten van Dijl, Michael Lalk, Ulrike Mäder, Jörg Stülke, Erhard Bremer, Uwe Völker, Christoph Wittmann
Adaptation of Bacillus subtilis carbon core metabolism to simultaneous nutrient limitation and osmotic challenge: a multi-omics perspective.
Environ Microbiol: 2014, 16(6);1898-917
[PubMed:24571712] [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)