SlrR

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  • 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
Gene expression levels in SubtiExpress: slrR
Interactions involving this protein in SubtInteract: SlrR
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
Sequences Protein DNA Advanced_DNA
Genetic context
Slr context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SlrR expression.png















Categories containing this gene/protein

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

This gene is a member of the following regulons

Abh regulon, AbrB regulon, SinR regulon

The SlrR regulon:

The gene

Basic information

  • Locus tag: BSU34380

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

  • overexpression of slrR suppresses the phenotype of a ymdB mutant PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • SlrR binds to and inhibits the activity of SlrA, SlrA indirectly stimulates the synthesis of SlrR by interacting with SinR. SlrR can bind to SinR and SinR directly represses the transcription of SlrR. SlrR indirectly derepresses its own gene. The heterocomplex of SlrR-SinR is a repressor of autolysin and motility genes and inhibits the repressor function of SinR. 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

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Additional information:
    • induction by sequestration of SinR by SinI, SlrA PubMed or by SlrR itself PubMed
    • the slrR gene 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

Biological materials

  • 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

Your additional remarks

References

Reviews

Original publications

Joseph A Newman, Cecilia Rodrigues, Richard J Lewis
Molecular basis of the activity of SinR protein, the master regulator of biofilm formation in Bacillus subtilis.
J Biol Chem: 2013, 288(15);10766-78
[PubMed:23430750] [WorldCat.org] [DOI] (I p)

Ying Lei, Taku Oshima, Naotake Ogasawara, Shu Ishikawa
Functional analysis of the protein Veg, which stimulates biofilm formation in Bacillus subtilis.
J Bacteriol: 2013, 195(8);1697-705
[PubMed:23378512] [WorldCat.org] [DOI] (I p)

Loralyn M Cozy, Andrew M Phillips, Rebecca A Calvo, Ashley R Bate, Yi-Huang Hsueh, Richard Bonneau, Patrick Eichenberger, Daniel B Kearns
SlrA/SinR/SlrR inhibits motility gene expression upstream of a hypersensitive and hysteretic switch at the level of σ(D) in Bacillus subtilis.
Mol Microbiol: 2012, 83(6);1210-28
[PubMed:22329926] [WorldCat.org] [DOI] (I p)

Eric R Pozsgai, Kris M Blair, Daniel B Kearns
Modified mariner transposons for random inducible-expression insertions and transcriptional reporter fusion insertions in Bacillus subtilis.
Appl Environ Microbiol: 2012, 78(3);778-85
[PubMed:22113911] [WorldCat.org] [DOI] (I p)

Christine Diethmaier, Nico Pietack, Katrin Gunka, Christoph Wrede, Martin Lehnik-Habrink, Christina Herzberg, Sebastian Hübner, Jörg Stülke
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] [WorldCat.org] [DOI] (I p)

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)

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