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
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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:

• lytA-lytB-lytC, lytF

The gene

Basic information

• Locus tag: BSU34380

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

• 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
  • the slrR gene is not expressed in a ymdB mutant PubMed

Biological materials

• Mutant:
  • GP955 (slrR-pnbA::cat), 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:

References

Original publications

Additional publications: PubMed

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

Patrice Bruscella, Karen Shahbabian, Soumaya Laalami, Harald Putzer
RNase Y is responsible for uncoupling the expression of translation factor IF3 from that of the ribosomal proteins L35 and L20 in Bacillus subtilis.
Mol Microbiol: 2011, 81(6);1526-41
[PubMed:21843271] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J Bacteriol: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Henrike Pförtner, Leonie Rempeters, Nico Pietack, Christina Herzberg, Jörg Stülke
The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex.
Mol Microbiol: 2010, 77(4);958-71
[PubMed:20572937] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Shiyi Yao, David H Bechhofer
Initiation of decay of Bacillus subtilis rpsO mRNA by endoribonuclease RNase Y.
J Bacteriol: 2010, 192(13);3279-86
[PubMed:20418391] [WorldCat.org] [DOI] (I p)

Jessica C Zweers, Thomas Wiegert, Jan Maarten van Dijl
Stress-responsive systems set specific limits to the overproduction of membrane proteins in Bacillus subtilis.
Appl Environ Microbiol: 2009, 75(23);7356-64
[PubMed:19820159] [WorldCat.org] [DOI] (I p)

Karen Shahbabian, Ailar Jamalli, Léna Zig, Harald Putzer
RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis.
EMBO J: 2009, 28(22);3523-33
[PubMed:19779461] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Alison Hunt, Joy P Rawlins, Helena B Thomaides, Jeff Errington
Functional analysis of 11 putative essential genes in Bacillus subtilis.
Microbiology (Reading): 2006, 152(Pt 10);2895-2907
[PubMed:17005971] [WorldCat.org] [DOI] (P p)