Difference between revisions of "EpsA"

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(Biological materials)
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
+
* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Mutant:'''  
 
* '''Mutant:'''  
** GP1517 (aphA3), available in [[Stülke]] lab
+
** GP1517 (aphA3), available in [[ Jörg Stülke]]'s lab
** GP1519 (epsAB, aphA3), available in [[Stülke]] lab  
+
** GP1519 (''[[epsA]]-[[epsB]]'', aphA3), available in [[ Jörg Stülke]]'s lab  
** GP1567 epsA::aphA3 tkmA::spc, available in [[Stülke]] lab
+
** GP1567 ''[[epsA]]''::aphA3 ''[[tkmA]]''::spc, available in [[ Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
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* '''GFP fusion:''' GP1569 epsA-gfp (spc)
 
* '''GFP fusion:''' GP1569 epsA-gfp (spc)
  
* '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab  
+
* '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[ Jörg Stülke]]'s lab  
  
 
* '''Antibody:'''
 
* '''Antibody:'''
  
* '''FLAG-tag construct:''' GP1526 epsA-FLAG 3x spc available in [[Stülke]] lab
+
* '''FLAG-tag construct:''' GP1526 epsA-FLAG 3x spc available in [[ Jörg Stülke]]'s lab
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=

Revision as of 10:29, 31 January 2014

  • Description: extracellular polysaccharide synthesis, putative transmembrane modulator of EpsB activity, might activate EpsB autophosphorylation and substrate phosphorylation

Gene name epsA
Synonyms yveK
Essential no
Product unknown
Function biofilm formation
Gene expression levels in SubtiExpress: epsA
Interactions involving this protein in SubtInteract: EpsA
Regulation of this protein in SubtiPathways:
epsA
MW, pI 25 kDa, 6.071
Gene length, protein length 702 bp, 234 aa
Immediate neighbours epsB, slrR
Sequences Protein DNA DNA_with_flanks
Genetic context
YveK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
EpsA expression.png















Categories containing this gene/protein

protein modification, biofilm formation, membrane proteins

This gene is a member of the following regulons

AbrB regulon, RemA regulon, SinR regulon

The gene

Basic information

  • Locus tag: BSU34370

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: cpsC/capA family (according to Swiss-Prot)
  • Paralogous protein(s): TkmA

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion: GP1569 epsA-gfp (spc)
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:
  • FLAG-tag construct: GP1526 epsA-FLAG 3x spc available in Jörg Stülke's lab

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

Your additional remarks

References

Reviews


Original publications

Jared T Winkelman, Anna C Bree, Ashley R Bate, Patrick Eichenberger, Richard L Gourse, Daniel B Kearns
RemA is a DNA-binding protein that activates biofilm matrix gene expression in Bacillus subtilis.
Mol Microbiol: 2013, 88(5);984-97
[PubMed:23646920] [WorldCat.org] [DOI] (I p)

Christine Diethmaier, Nico Pietack, Katrin Gunka, Christoph Wrede, Martin Lehnik-Habrink, Christina Herzberg, Sebastian Hübner, Jörg Stülke
A novel factor controlling bistability in Bacillus subtilis: the YmdB protein affects flagellin expression and biofilm formation.
J Bacteriol: 2011, 193(21);5997-6007
[PubMed:21856853] [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)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
An epigenetic switch governing daughter cell separation in Bacillus subtilis.
Genes Dev: 2010, 24(8);754-65
[PubMed:20351052] [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)