AbrB

• Description: transcriptional regulator of transition state genes
  
  

Gene name	abrB
Synonyms	cpsX, tolB
Essential	no
Product	transcriptional regulator
Function	regulation of gene expression during the transition from growth to stationary phase
Gene expression levels in SubtiExpress: abrB
Interactions involving this protein in SubtInteract: AbrB
Metabolic function and regulation of this protein in SubtiPathways: abrB
MW, pI	10 kDa, 6.57
Gene length, protein length	282 bp, 94 aa
Immediate neighbours	yabC, metS
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

transition state regulators

This gene is a member of the following regulons

AbrB regulon, Spo0A regulon

The gene

Basic information

• Locus tag: BSU00370

Phenotypes of a mutant

• No swarming motility on B medium PubMed

Database entries

• BsubCyc: BSU00370

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): Abh, SpoVT (only N-terminal domain)

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on Ser-86 PubMed by PrkC, PrkD, and YabT results in loss of DNA-binding activity PubMed

• Cofactors:

• Effectors of protein activity: interaction with AbbA results in inactivation of AbrB PubMed

• Interactions:
  • AbbA-AbrB, AbbA binds the N-terminal DNA-binding domain of AbrB PubMed
  • AbrB-AbrB PubMed
  • AbrB-Abh PubMed
  • AbrB-PrkC PubMed
  • AbrB-PrkD PubMed
  • AbrB-YabT PubMed

• Localization:

Database entries

• BsubCyc: BSU00370

• Structure:
  • 1Z0R (N-terminal DNA recognition domain), PubMed
  • 2MJG (full-length protein) PubMed

• UniProt: P08874

• KEGG entry: [3]

Expression and regulation

• Operon: abrB PubMed

• Expression browser: abrB PubMed

• Sigma factor: SigA PubMed

• Regulation: expressed at the onset of stationary phase PubMed
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • repressed during logrithmic growth (AbrB) PubMed

• Regulatory mechanism: repressed by Spo0A-P PubMed
  • Spo0A: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2859 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 10811 PubMed

Biological materials

• Mutant: TT731 (aphA3)
  • 1A935 (abrB::cat), PubMed, available at BGSC
  • GP1548 (abrB::ermC), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

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

• Antibody:

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

Mark Strauch, Baltimore, USA homepage

References

Reviews

Daniel Schultz, Peter G Wolynes, Eshel Ben Jacob, José N Onuchic
Deciding fate in adverse times: sporulation and competence in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2009, 106(50);21027-34
[PubMed:19995980] [WorldCat.org] [DOI] (I p)

Kassem Hamze, Daria Julkowska, Sabine Autret, Krzysztof Hinc, Krzysztofa Nagorska, Agnieszka Sekowska, I Barry Holland, Simone J Séror
Identification of genes required for different stages of dendritic swarming in Bacillus subtilis, with a novel role for phrC.
Microbiology (Reading): 2009, 155(Pt 2);398-412
[PubMed:19202088] [WorldCat.org] [DOI] (P p)

Krzysztofa Nagórska, Krzysztof Hinc, Mark A Strauch, Michał Obuchowski
Influence of the sigmaB stress factor and yxaB, the gene for a putative exopolysaccharide synthase under sigmaB Control, on biofilm formation.
J Bacteriol: 2008, 190(10);3546-56
[PubMed:18326573] [WorldCat.org] [DOI] (I p)

Z E V Phillips, M A Strauch
Bacillus subtilis sporulation and stationary phase gene expression.
Cell Mol Life Sci: 2002, 59(3);392-402
[PubMed:11964117] [WorldCat.org] [DOI] (P p)

Wolfgang Klein, Mohamed A Marahiel
Structure-function relationship and regulation of two Bacillus subtilis DNA-binding proteins, HBsu and AbrB.
J Mol Microbiol Biotechnol: 2002, 4(3);323-9
[PubMed:11931565] [WorldCat.org] (P p)