Des

• Description: phospholipid desaturase
  
  

Gene name	des
Synonyms	yocE
Essential	no
Product	phospholipid desaturase
Function	adaptation of membrane fluidity at low temperatures
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation
MW, pI	40 kDa, 9.88
Gene length, protein length	1056 bp, 352 aa
Immediate neighbours	yocD, desK
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU19180

Phenotypes of a mutant

cold-sensitive PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: O34653

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: des PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced upon cold shock (DesR) PubMed
  • repressed at increased membrane fluidity PubMed

• Regulatory mechanism:
  • two component system DesR-DesK: transcription activation PubMed, PubMed

• 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

References

Jana Beranová, María C Mansilla, Diego de Mendoza, Dana Elhottová, Ivo Konopásek
Differences in cold adaptation of Bacillus subtilis under anaerobic and aerobic conditions.
J Bacteriol: 2010, 192(16);4164-71
[PubMed:20581210] [WorldCat.org] [DOI] (I p)

Natalia Martin, Esteban Lombardía, Silvia G Altabe, Diego de Mendoza, María C Mansilla
A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis.
J Bacteriol: 2009, 191(24);7447-55
[PubMed:19820084] [WorldCat.org] [DOI] (I p)

Anna-Barbara Hachmann, Esther R Angert, John D Helmann
Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin.
Antimicrob Agents Chemother: 2009, 53(4);1598-609
[PubMed:19164152] [WorldCat.org] [DOI] (I p)

Silvia G Altabe, Pablo Aguilar, Gerardo M Caballero, Diego de Mendoza
The Bacillus subtilis acyl lipid desaturase is a delta5 desaturase.
J Bacteriol: 2003, 185(10);3228-31
[PubMed:12730185] [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)

M H Weber, W Klein, L Müller, U M Niess, M A Marahiel
Role of the Bacillus subtilis fatty acid desaturase in membrane adaptation during cold shock.
Mol Microbiol: 2001, 39(5);1321-9
[PubMed:11251847] [WorldCat.org] [DOI] (P p)

P S Aguilar, P Lopez, D de Mendoza
Transcriptional control of the low-temperature-inducible des gene, encoding the delta5 desaturase of Bacillus subtilis.
J Bacteriol: 1999, 181(22);7028-33
[PubMed:10559169] [WorldCat.org] [DOI] (P p)

P S Aguilar, J E Cronan, D de Mendoza
A Bacillus subtilis gene induced by cold shock encodes a membrane phospholipid desaturase.
J Bacteriol: 1998, 180(8);2194-200
[PubMed:9555904] [WorldCat.org] [DOI] (P p)

Additional papers

PubMed