EpsH

• Description: extracellular polysaccharide synthesis
  
  

Gene name	epsH
Synonyms	yveR
Essential	no
Product	unknown
Function	biofilm formation
Regulation of this protein in SubtiPathways: Biofilm
MW, pI	39 kDa, 5.788
Gene length, protein length	1032 bp, 344 aa
Immediate neighbours	epsI, epsG
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biofilm formation

This gene is a member of the following regulons

AbrB regulon, EAR riboswitch, SinR regulon

The gene

Basic information

• Locus tag: BSU34300

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• 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:

• Localization:

Database entries

• Structure:

• UniProt: P71057

• 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

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by SinR PubMed

• Regulatory mechanism:
  • SinR: transcription repression 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 PubMed

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

References

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