EpsE

• Description: inhibitor of motility and glycosyltransferase required for EPS biosynthesis
  
  

Gene name	epsE
Synonyms	yveO
Essential	no
Product	glycosyltransferase, inhibitor of motility
Function	biofilm formation
Gene expression levels in SubtiExpress: epsE
Interactions involving this protein in SubtInteract: EpsE
Regulation of this protein in SubtiPathways: epsE
MW, pI	32 kDa, 9.804
Gene length, protein length	834 bp, 278 aa
Immediate neighbours	epsF, epsD
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

motility and chemotaxis, biofilm formation, membrane proteins

This gene is a member of the following regulons

AbrB regulon, EAR riboswitch, RemA regulon, SinR regulon

The gene

Basic information

• Locus tag: BSU34330

Phenotypes of a mutant

• • smooth colonies on MsGG medium, no biofilm formation PubMed

Database entries

• BsubCyc: BSU34330

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • arrests flagellar rotation in a manner similar to that of a clutch, by disengaging motor force-generating elements in cells embedded in the biofilm matrix, separates the cytoplasmic FliG motor from the MotA-MotB stator PubMed
  • biosynthesis of extracellular polysaccharides PubMed

• Protein family: glycosyltransferase 2 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • EpsE-FliG PubMed

• Localization: cell membrane, forms spots at flagellar basal bodies PubMed

Database entries

• BsubCyc: BSU34330

• Structure:

• UniProt: P71054

• 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: epsE 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
  • the EAR riboswitch (eps-associated RNA switch) located between epsB and epsC mediates processive antitermination and allows expression of the long eps operon PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Daniel Kearns, Indiana University, Bloomington, USA, homepage
• Richard Losick, Harvard Univ., Cambridge, USA homepage

References

Reviews

Lynne S Cairns, Laura Hobley, Nicola R Stanley-Wall
Biofilm formation by Bacillus subtilis: new insights into regulatory strategies and assembly mechanisms.
Mol Microbiol: 2014, 93(4);587-98
[PubMed:24988880] [WorldCat.org] [DOI] (I p)

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

The EAR RNA switch

Irnov Irnov, Wade C Winkler
A regulatory RNA required for antitermination of biofilm and capsular polysaccharide operons in Bacillales.
Mol Microbiol: 2010, 76(3);559-75
[PubMed:20374491] [WorldCat.org] [DOI] (I p)

Zasha Weinberg, Joy X Wang, Jarrod Bogue, Jingying Yang, Keith Corbino, Ryan H Moy, Ronald R Breaker
Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea, and their metagenomes.
Genome Biol: 2010, 11(3);R31
[PubMed:20230605] [WorldCat.org] [DOI] (I p)