DegU

• Description: two-component response regulator, regulation of degradative enzyme expression, genetic competence, biofilm formation, capsule biosynthesis (together with SwrAA), non-phosphorylated DegU is required for swarming motility
  
  

Gene name	degU
Synonyms	sacU, iep
Essential	no
Product	two-component response regulator
Function	regulation of degradative enzymes, genetic competence, biofilm formation and capsule synthesis
Gene expression levels in SubtiExpress: degU
Interactions involving this protein in SubtInteract: DegU
Metabolic function and regulation of this protein in SubtiPathways: DegU
MW, pI	25 kDa, 5.602
Gene length, protein length	687 bp, 229 aa
Immediate neighbours	yviA, degS
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

biofilm formation, transcription factors and their control, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, DegU regulon, SinR regulon, TnrA regulon

The gene

Basic information

• Locus tag: BSU35490

Phenotypes of a mutant

• defect in biofilm formation PubMed, this can be suppressed by DegU-independent expression of BslA PubMed
• the mutation suppresses the mucoid phenotype of motA or motB mutants due to reduced expression of the capB-capC-capA-capE operon PubMed

Database entries

• BsubCyc: BSU35490

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • transcription activator and repressor (see DegU regulon)
  • DegU-P represses expression of the fla/che operon (flgB-flgC-fliE-fliF-fliG-fliH-fliI-fliJ-ylxF-fliK-flgD-flgE-fliL-fliM-fliY-cheY-fliZ-fliP-fliQ-fliR-flhB-flhA-flhF-flhG-cheB-cheA-cheW-cheC-cheD-sigD-swrB) in the absence of SwrA, and switches to an activator of the operon in the presence of SwrA PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated by DegS on Asp-56 PubMed, this modulates DNA-binding activity
  • phosphorylation by DegS occurs in response to inhibition of flagellar rotation PubMed

• Cofactors:

• Effectors of protein activity:
  • DNA-binding activity of DegU is inhibited by RapG PubMed
  • DegU-P is degraded by ClpC-ClpP PubMed

• Interactions:
  • DegU-RapG PubMed
  • DegS-DegU
  • SwrA-DegU-P (N-terminal domain) PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU35490

• Structure:

• UniProt: P13800

• KEGG entry: [3]

• E.C. number:

Additional information

• DegU-P is degraded by ClpC-ClpP PubMed
• accumulation of DegU-P results in decreased transcription of the epsA-epsO and tapA-sipW-tasA operons due to increased levels of Spo0A-P PubMed

Expression and regulation

• Operon:
  • degS-degU PubMed
  • degU PubMed

• Expression browser: degU PubMed

• Sigma factor:
  • degS: SigA PubMed
  • degU: SigA PubMed

• Regulation:
  • induced in the presence of ammonium (TnrA) PubMed
  • induced by glucose (CcpA) PubMed

• Regulatory mechanism:
  • DegU: positive autoregulation PubMed
  • TnrA: transcription repression PubMed
  • CcpA: transcription activation PubMed
  • SinR: transcription repression PubMed

• Additional information:
  • DegU-P is degraded by ClpC-ClpP PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1627 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2454 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2251 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1461 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1432 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• Antibody:

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)

Robert Belas
When the swimming gets tough, the tough form a biofilm.
Mol Microbiol: 2013, 90(1);1-5
[PubMed:23927648] [WorldCat.org] [DOI] (I p)

Daniel López, Roberto Kolter
Extracellular signals that define distinct and coexisting cell fates in Bacillus subtilis.
FEMS Microbiol Rev: 2010, 34(2);134-49
[PubMed:20030732] [WorldCat.org] [DOI] (I p)

Ewan J Murray, Taryn B Kiley, Nicola R Stanley-Wall
A pivotal role for the response regulator DegU in controlling multicellular behaviour.
Microbiology (Reading): 2009, 155(Pt 1);1-8
[PubMed:19118340] [WorldCat.org] [DOI] (P p)

The DegU regulon

U Mäder, H Antelmann, T Buder, M K Dahl, M Hecker, G Homuth
Bacillus subtilis functional genomics: genome-wide analysis of the DegS-DegU regulon by transcriptomics and proteomics.
Mol Genet Genomics: 2002, 268(4);455-67
[PubMed:12471443] [WorldCat.org] [DOI] (P p)