Difference between revisions of "SlrR"
(→Extended information on the protein) |
|||
Line 126: | Line 126: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
** induction by sequestration of [[SinR]] by [[SinI]], [[SlrA]] {{PubMed|15661000,19788541}} or by SlrR itself {{PubMed|20351052}} | ** induction by sequestration of [[SinR]] by [[SinI]], [[SlrA]] {{PubMed|15661000,19788541}} or by SlrR itself {{PubMed|20351052}} | ||
+ | ** the ''[[slrR]]'' gene is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}} | ||
=Biological materials = | =Biological materials = | ||
Line 150: | Line 151: | ||
==Original publications== | ==Original publications== | ||
'''Additional publications:''' {{PubMed|20817675}} | '''Additional publications:''' {{PubMed|20817675}} | ||
+ | <big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J'' </big> | ||
+ | <big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big> | ||
+ | <big>Flagellin Expression and Biofilm Formation.''' </big> | ||
+ | J Bacteriol. 2011 Aug 19. [Epub ahead of print] | ||
+ | [http://www.ncbi.nlm.nih.gov/pubmed/21856853 PubMed:21856853] | ||
+ | |||
+ | <pubmed>18763711,19193632,17005971 19779461 19820159 20418391 20525796 20572937,21803996 21843271 </pubmed> | ||
<pubmed>18430133,18647168, 19767430, 19788541 20351052 20923420 </pubmed> | <pubmed>18430133,18647168, 19767430, 19788541 20351052 20923420 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:34, 23 August 2011
- 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
|
Contents
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
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:
- 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:
- UniProt: P71049
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
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:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Patrick Piggot
Epigenetic switching: bacteria hedge bets about staying or moving.
Curr Biol: 2010, 20(11);R480-2
[PubMed:20541494]
[WorldCat.org]
[DOI]
(I p)
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 Aug 19. [Epub ahead of print] PubMed:21856853