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"| '''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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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 22 kDa, 4.885 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 22 kDa, 4.885 |
Revision as of 13:51, 16 February 2010
- 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 |
Metabolic function and regulation of this protein in SubtiPathways: Fatty acid degradation | |
MW, pI | 22 kDa, 4.885 |
Gene length, protein length | 597 bp, 199 aa |
Immediate neighbours | desK, yocH |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
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:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O34723
- 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
- Diego de Mendoza, Universidad Nacional de Rosario, Argentine homepage
Your additional remarks
References
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)