Difference between revisions of "EpsE"
| Line 90: | Line 90: | ||
=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[epsA]]-[[epsB]]-[[epsC]]-[[epsD]]-[[epsE]]-[[epsF]]-[[epsG]]-[[epsH]]-[[epsI]]-[[epsJ]]-[[epsK]]-[[epsL]]-[[epsM]]-[[epsN]]-[[epsO]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] |
| − | * '''[[Sigma factor]]:''' | + | * '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] |
* '''Regulation:''' | * '''Regulation:''' | ||
| − | * '''Regulatory mechanism:''' | + | * '''Regulatory mechanism:''' [[SinR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] |
| − | * '''Additional information:''' | + | * '''Additional information:''' induction by sequestration of [[SinR]] by [[SinI]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] |
=Biological materials = | =Biological materials = | ||
| Line 115: | Line 115: | ||
=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
| + | |||
| + | [[Richard Losick]], Harvard Univ., Cambridge, USA [http://www.mcb.harvard.edu/Losick/ homepage] | ||
=Your additional remarks= | =Your additional remarks= | ||
=References= | =References= | ||
| + | |||
| + | <pubmed>16430695,18047568,15661000</pubmed> | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | ||
Revision as of 18:06, 31 May 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
- Coordinates:
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: BSU34330
- E.C. number:
Additional information
Expression and regulation
- 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
