Difference between revisions of "PksR"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU17220&redirect=T BSU17220] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU17220&redirect=T BSU17220] | ||
* '''Structure:''' | * '''Structure:''' |
Revision as of 13:48, 2 April 2014
- Description: polyketide synthase
Gene name | pksR |
Synonyms | |
Essential | no |
Product | polyketide synthase |
Function | polyketide synthesis |
Gene expression levels in SubtiExpress: pksR | |
MW, pI | 284 kDa, 5.437 |
Gene length, protein length | 7629 bp, 2543 aa |
Immediate neighbours | pksN, pksS |
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
miscellaneous metabolic pathways, biosynthesis of antibacterial compounds
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU17220
Phenotypes of a mutant
Database entries
- BsubCyc: BSU17220
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU17220
- Structure:
- UniProt: O31784
- KEGG entry: [2]
- 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
Carol Vargas-Bautista, Kathryn Rahlwes, Paul Straight
Bacterial competition reveals differential regulation of the pks genes by Bacillus subtilis.
J Bacteriol: 2014, 196(4);717-28
[PubMed:24187085]
[WorldCat.org]
[DOI]
(I p)
Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849]
[WorldCat.org]
[DOI]
(I p)
Paul D Straight, Michael A Fischbach, Christopher T Walsh, David Z Rudner, Roberto Kolter
A singular enzymatic megacomplex from Bacillus subtilis.
Proc Natl Acad Sci U S A: 2007, 104(1);305-10
[PubMed:17190806]
[WorldCat.org]
[DOI]
(P p)
M S Turner, J D Helmann
Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis.
J Bacteriol: 2000, 182(18);5202-10
[PubMed:10960106]
[WorldCat.org]
[DOI]
(P p)