Difference between revisions of "YfmG"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU07480&redirect=T BSU07480] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yfmG.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yfmG.html] | ||
Line 87: | Line 88: | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU07480&redirect=T BSU07480] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 13:11, 2 April 2014
- Description: unknown
Gene name | yfmG |
Synonyms | |
Essential | no |
Product | unknown |
Function | unknown |
Gene expression levels in SubtiExpress: yfmG | |
MW, pI | 56 kDa, 5.185 |
Gene length, protein length | 1461 bp, 487 aa |
Immediate neighbours | yfmI, yfmF |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
proteins of unknown function, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU07480
Phenotypes of a mutant
Database entries
- BsubCyc: BSU07480
- 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:
- phosphorylated on Arg-474 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- BsubCyc: BSU07480
- Structure:
- UniProt: O34722
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- repressed by glucose (4-fold) PubMed
- 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
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947]
[WorldCat.org]
[DOI]
(I p)
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796]
[WorldCat.org]
[DOI]
(I p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)