SinR

• Description: transcriptional regulator of post-exponential-phase responses genes
  
  

Gene name	sinR
Synonyms	sin, flaD
Essential	no
Product	transcriptional regulator of post-exponential-phase responses genes
Function	regulation of post-exponential gene expression
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	12 kDa, 7.177
Gene length, protein length	333 bp, 111 aa
Immediate neighbours	sinI, tasA
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: BSU24610

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): SlrR

Genes controlled by SinR

• Activation by SinR: comK

• Repression by SinR: aprE, kinB, rapG PubMed, sigD, spo0A,spoIIAA-spoIIAB-sigF, spoIIE, spoIIGA-sigE-sigG, spoVG PubMed, yqxM-sipW-tasA PubMed, yvgN PubMed, ywbD PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: SinI and SlrA are antagonists to SinR PubMed

• Interactions: SlrA-SinR PubMed, SinR-ScoC, SinR-SinI

• Localization:

Database entries

• Structure: 1B0N (complex SinR-SinI)

• UniProt: P06533

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sinI-sinR PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • repressed during exponential growth (ScoC) PubMed
  • repressed during logrithmic growth (AbrB) PubMed

• Regulatory mechanism:
  • Spo0A: transcription repression PubMed
  • ScoC: transcription repression PubMed
  • AbrB: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Prashant Kodgire, K Krishnamurthy Rao
A dual mode of regulation of flgM by ScoC in Bacillus subtilis.
Can J Microbiol: 2009, 55(8);983-9
[PubMed:19898538] [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)

Yunrong Chai, Roberto Kolter, Richard Losick
A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation.
J Bacteriol: 2009, 191(8);2423-30
[PubMed:19201793] [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)

Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568] [WorldCat.org] [DOI] (P p)

Prashant Kodgire, Madhulika Dixit, K Krishnamurthy Rao
ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis.
J Bacteriol: 2006, 188(17);6425-8
[PubMed:16923912] [WorldCat.org] [DOI] (P p)

Steven S Branda, Frances Chu, Daniel B Kearns, Richard Losick, Roberto Kolter
A major protein component of the Bacillus subtilis biofilm matrix.
Mol Microbiol: 2006, 59(4);1229-38
[PubMed:16430696] [WorldCat.org] [DOI] (P p)

Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695] [WorldCat.org] [DOI] (P p)

Daniel B Kearns, Frances Chu, Steven S Branda, Roberto Kolter, Richard Losick
A master regulator for biofilm formation by Bacillus subtilis.
Mol Microbiol: 2005, 55(3);739-49
[PubMed:15661000] [WorldCat.org] [DOI] (P p)

Alejandro Sánchez, Jorge Olmos
Bacillus subtilis transcriptional regulators interaction.
Biotechnol Lett: 2004, 26(5);403-7
[PubMed:15104138] [WorldCat.org] [DOI] (P p)

Sasha H Shafikhani, Ines Mandic-Mulec, Mark A Strauch, Issar Smith, Terrance Leighton
Postexponential regulation of sin operon expression in Bacillus subtilis.
J Bacteriol: 2002, 184(2);564-71
[PubMed:11751836] [WorldCat.org] [DOI] (P p)

D J Scott, S Leejeerajumnean, J A Brannigan, R J Lewis, A J Wilkinson, J G Hoggett
Quaternary re-arrangement analysed by spectral enhancement: the interaction of a sporulation repressor with its antagonist.
J Mol Biol: 1999, 293(5);997-1004
[PubMed:10547280] [WorldCat.org] [DOI] (P p)

R J Lewis, J A Brannigan, W A Offen, I Smith, A J Wilkinson
An evolutionary link between sporulation and prophage induction in the structure of a repressor:anti-repressor complex.
J Mol Biol: 1998, 283(5);907-12
[PubMed:9799632] [WorldCat.org] [DOI] (P p)

K Fredrick, J D Helmann
FlgM is a primary regulator of sigmaD activity, and its absence restores motility to a sinR mutant.
J Bacteriol: 1996, 178(23);7010-3
[PubMed:8955328] [WorldCat.org] [DOI] (P p)

J Hahn, A Luttinger, D Dubnau
Regulatory inputs for the synthesis of ComK, the competence transcription factor of Bacillus subtilis.
Mol Microbiol: 1996, 21(4);763-75
[PubMed:8878039] [WorldCat.org] [DOI] (P p)

M A Strauch
In vitro binding affinity of the Bacillus subtilis AbrB protein to six different DNA target regions.
J Bacteriol: 1995, 177(15);4532-6
[PubMed:7635837] [WorldCat.org] [DOI] (P p)

P T Kallio, J E Fagelson, J A Hoch, M A Strauch
The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein.
J Biol Chem: 1991, 266(20);13411-7
[PubMed:1906467] [WorldCat.org] (P p)

N K Gaur, K Cabane, I Smith
Structure and expression of the Bacillus subtilis sin operon.
J Bacteriol: 1988, 170(3);1046-53
[PubMed:3125149] [WorldCat.org] [DOI] (P p)