Difference between revisions of "EpsG"
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
** [[SinR]]: transcription repression {{PubMed|15661000}} | ** [[SinR]]: transcription repression {{PubMed|15661000}} | ||
+ | ** [[AbrB]]: transcription repression {{PubMed|20817675}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
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<pubmed>20735481 </pubmed> | <pubmed>20735481 </pubmed> | ||
==Original publications== | ==Original publications== | ||
− | <pubmed>15661000,16430695,18047568,11572999 18647168 </pubmed> | + | <pubmed>15661000,16430695,18047568,11572999 18647168 20817675</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:28, 15 September 2010
- Description: extracellular polysaccharide synthesis
Gene name | epsG |
Synonyms | yveQ |
Essential | no |
Product | unknown |
Function | extracellular polysaccharide synthesis |
Regulation of this protein in SubtiPathways: Biofilm | |
MW, pI | 42 kDa, 9.379 |
Gene length, protein length | 1101 bp, 367 aa |
Immediate neighbours | epsH, epsF |
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: BSU34310
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:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P71056
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Richard Losick, Harvard Univ., Cambridge, USA homepage
Your additional remarks
References
Reviews
Original publications
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)
Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168]
[WorldCat.org]
[DOI]
(I p)
Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568]
[WorldCat.org]
[DOI]
(P p)
Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695]
[WorldCat.org]
[DOI]
(P p)
Daniel B Kearns, Frances Chu, Steven S Branda, Roberto Kolter, Richard Losick
A master regulator for biofilm formation by Bacillus subtilis.
Mol Microbiol: 2005, 55(3);739-49
[PubMed:15661000]
[WorldCat.org]
[DOI]
(P p)
S S Branda, J E González-Pastor, S Ben-Yehuda, R Losick, R Kolter
Fruiting body formation by Bacillus subtilis.
Proc Natl Acad Sci U S A: 2001, 98(20);11621-6
[PubMed:11572999]
[WorldCat.org]
[DOI]
(P p)