Difference between revisions of "EpsB"

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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed>20735481 20351052 </pubmed>
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<pubmed>20735481 </pubmed>
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==Original publications==
 
==Original publications==
 
<pubmed>15661000,16430695,18047568,18647168 18547145 </pubmed>
 
<pubmed>15661000,16430695,18047568,18647168 18547145 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:01, 26 August 2010

  • Description: extracellular polysaccharide synthesis, putative protein tyrosine kinase

Gene name epsB
Synonyms yveL
Essential no
Product unknown
Function extracellular polysaccharide synthesis
Regulation of this protein in SubtiPathways:
Biofilm
MW, pI 24 kDa, 9.918
Gene length, protein length 681 bp, 227 aa
Immediate neighbours epsC, epsA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YveL context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU34360

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate (according to Swiss-Prot)
  • Protein family: cpsD/capB family (according to Swiss-Prot)
  • Paralogous protein(s): PtkA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure: 2VED (CapB, the homolog in Staphylococcus aureus) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:

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

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)

Vanesa Olivares-Illana, Philippe Meyer, Emmanuelle Bechet, Virginie Gueguen-Chaignon, Didier Soulat, Sylvie Lazereg-Riquier, Ivan Mijakovic, Josef Deutscher, Alain J Cozzone, Olivier Laprévote, Solange Morera, Christophe Grangeasse, Sylvie Nessler
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus.
PLoS Biol: 2008, 6(6);e143
[PubMed:18547145] [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)