Difference between revisions of "YdhF"
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* '''Operon:''' ''[[phoB]]-[[ydhF]]'' {{PubMed|10913081}} | * '''Operon:''' ''[[phoB]]-[[ydhF]]'' {{PubMed|10913081}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ydhF_619321_620031_-1 ydhF] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' [[SigA]], [[SigE]] {{PubMed|15699190,16030210}} | ||
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 15:10, 12 April 2012
- Description: unknown
Gene name | ydhF |
Synonyms | |
Essential | no |
Product | unknown |
Function | unknown |
Metabolic function and regulation of this protein in SubtiPathways: Folate | |
MW, pI | 26 kDa, 6.155 |
Gene length, protein length | 708 bp, 236 aa |
Immediate neighbours | ydhE, phoB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU05730
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
- Localization: extracellular (signal peptide) PubMed, lipid modification as retention signal
Database entries
- Structure:
- UniProt: O05497
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Wael R Abdel-Fattah, Yinghua Chen, Amr Eldakak, F Marion Hulett
Bacillus subtilis phosphorylated PhoP: direct activation of the E(sigma)A- and repression of the E(sigma)E-responsive phoB-PS+V promoters during pho response.
J Bacteriol: 2005, 187(15);5166-78
[PubMed:16030210]
[WorldCat.org]
[DOI]
(P p)
H Antelmann, C Scharf, M Hecker
Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis.
J Bacteriol: 2000, 182(16);4478-90
[PubMed:10913081]
[WorldCat.org]
[DOI]
(P p)
W Liu, F M Hulett
Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter.
J Bacteriol: 1997, 179(20);6302-10
[PubMed:9335276]
[WorldCat.org]
[DOI]
(P p)