Difference between revisions of "EpsB"

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(Expression and regulation)
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** induction by sequestration of [[SinR]] by [[SinI]] or [[SlrA]] {{PubMed|15661000,19788541}}
 
** induction by sequestration of [[SinR]] by [[SinI]] or [[SlrA]] {{PubMed|15661000,19788541}}
 
** the ''[[epsA]]-[[epsB]]-[[epsC]]-[[epsD]]-[[epsE]]-[[epsF]]-[[epsG]]-[[epsH]]-[[epsI]]-[[epsJ]]-[[epsK]]-[[epsL]]-[[epsM]]-[[epsN]]-[[epsO]]'' operon is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}}  
 
** the ''[[epsA]]-[[epsB]]-[[epsC]]-[[epsD]]-[[epsE]]-[[epsF]]-[[epsG]]-[[epsH]]-[[epsI]]-[[epsJ]]-[[epsK]]-[[epsL]]-[[epsM]]-[[epsN]]-[[epsO]]'' operon is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}}  
** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}}
+
** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] (this is likely due to the increased stability of the ''[[sinR]]'' mRNA) {{PubMed|21815947}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 14:05, 20 November 2011

  • Description: extracellular polysaccharide synthesis, putative protein tyrosine kinase

Gene name epsB
Synonyms yveL
Essential no
Product unknown
Function biofilm formation
Interactions involving this protein in SubtInteract: EpsB
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







Categories containing this gene/protein

protein modification, biofilm formation

This gene is a member of the following regulons

AbrB regulon, SinR regulon

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)
  • Paralogous protein(s): PtkA

Extended information on the protein

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

Database entries

  • Structure: 2VED (CapB, the homolog in Staphylococcus aureus) PubMed
  • 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

Reviews

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)


Original publications

Additional publications: PubMed

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947
Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J  
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

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)