Difference between revisions of "EpsE"
Line 95: | Line 95: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
+ | ** repressed by [[SinR]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] | ||
* '''Regulatory mechanism:''' [[SinR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] | * '''Regulatory mechanism:''' [[SinR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] | ||
+ | ** [[SinR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] | ||
* '''Additional information:''' induction by sequestration of [[SinR]] by [[SinI]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] | * '''Additional information:''' induction by sequestration of [[SinR]] by [[SinI]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] |
Revision as of 17:21, 11 June 2009
- Description: similar to glycosyltransferase
Gene name | epsE |
Synonyms | yveO |
Essential | no |
Product | unknown |
Function | extracellular polysaccharide synthesis |
MW, pI | 32 kDa, 9.804 |
Gene length, protein length | 834 bp, 278 aa |
Immediate neighbours | epsF, epsD |
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: BSU34330
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: glycosyltransferase 2 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P71054
- 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
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)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed