EpsB

• Description: extracellular polysaccharide synthesis, putative protein tyrosine kinase
  
  

Gene name	epsB
Synonyms	yveL
Essential	no
Product	unknown
Function	biofilm formation
Gene expression levels in SubtiExpress: epsB
Interactions involving this protein in SubtInteract: EpsB
Regulation of this protein in SubtiPathways: epsB
MW, pI	24 kDa, 9.918
Gene length, protein length	681 bp, 227 aa
Immediate neighbours	epsC, epsA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein modification, biofilm formation

This gene is a member of the following regulons

AbrB regulon, RemA regulon, SinR regulon

The gene

Basic information

• Locus tag: BSU34360

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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: BY kinase, see the Bacterial Protein Tyrosine Kinase Database)

• Paralogous protein(s): PtkA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • EpsA-EpsB (based on TkmA-PtkA interaction)

• Localization:

Database entries

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

• UniProt: P71051

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: epsA-epsB-epsC-epsD-epsE-epsF-epsG-epsH-epsI-epsJ-epsK-epsL-epsM-epsN-epsO PubMed

• Expression browser: epsB PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by SinR PubMed

• Regulatory mechanism:
  • SinR: transcription anti-activation (prevents binding of RemA) PubMed
  • RemA: transcription activation PubMed
  • AbrB: transcription repression PubMed

• Additional information:
  • induction by sequestration of SinR by SinI or SlrA PubMed
  • 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
  • the amount of the mRNA is substantially decreased upon depletion of RNase Y (this is likely due to the increased stability of the sinR mRNA) PubMed

Biological materials

• Mutant:

GP1518 (aphA3), available in Stülke lab GP1519 (epsAB, aphA3), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

• FLAG-tag construct: GP1541 (epsB-3xFLAG spc trpC2) , available in Jörg Stülke's lab

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

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

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)

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)