SlrR

• Description: transcriptional activator of competence development and sporulation genes, represses SigD-dependent flagellar genes, antagonist of SlrA and SinR, has LexA-like autocleavage activity
  
  

Gene name	slrR
Synonyms	yveJ, slr
Essential	no
Product	transcription regulator, SlrA antagonist
Function	regulation of initiation of biofilm formation and of autolysis
Regulation of this protein in SubtiPathways: Biofilm
MW, pI	17 kDa, 9.63
Gene length, protein length	456 bp, 152 aa
Immediate neighbours	epsA, pnbA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU34380

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

Categories containing this gene/protein

transcription factors and their control, transition state regulators, biofilm formation

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • binding and concomintant inactivation of SlrA results in release of SinR from the SinR-SlrA complex and subsequent induction of SinR-controlled genes and operons for biofilm formation PubMed
  • repression of transcription of lytA-lytB-lytC and lytF PubMed
  • autocleavage PubMed

• Protein family:

• Paralogous protein(s): SinR

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • subject to self-cleavage via a LexA-like autopeptidase, this involves ClpC PubMed

• Cofactor(s):

• Effectors of protein activity: interaction with SinR triggers binding of SlrR to the promoters of lytA-lytB-lytC and lytF, resulting in their repression PubMed

• Interactions:
  • SlrA-SlrR PubMed
  • SinR-SlrR PubMed

• Localization:

Database entries

• Structure:

• UniProt: P71049

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:
  • Abh: transcription activation PubMed
  • SinR: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:
  • induction by sequestration of SinR by SinI, SlrA PubMed or by SlrR itself 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 Stülke lab

• Antibody:

References

Original publications

Yunrong Chai, Roberto Kolter, Richard Losick
Reversal of an epigenetic switch governing cell chaining in Bacillus subtilis by protein instability.
Mol Microbiol: 2010, 78(1);218-29
[PubMed:20923420] [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)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
An epigenetic switch governing daughter cell separation in Bacillus subtilis.
Genes Dev: 2010, 24(8);754-65
[PubMed:20351052] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Roberto Kolter, Richard Losick
Paralogous antirepressors acting on the master regulator for biofilm formation in Bacillus subtilis.
Mol Microbiol: 2009, 74(4);876-87
[PubMed:19788541] [WorldCat.org] [DOI] (I p)

Ewan J Murray, Mark A Strauch, Nicola R Stanley-Wall
SigmaX is involved in controlling Bacillus subtilis biofilm architecture through the AbrB homologue Abh.
J Bacteriol: 2009, 191(22);6822-32
[PubMed:19767430] [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)

Frances Chu, Daniel B Kearns, Anna McLoon, Yunrong Chai, Roberto Kolter, Richard Losick
A novel regulatory protein governing biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 68(5);1117-27
[PubMed:18430133] [WorldCat.org] [DOI] (I p)