Difference between revisions of "LiaR"

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(Extended information on the protein)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' [[LiaS]]-[[LiaR]]
+
* '''[[SubtInteract|Interactions]]:'''
 +
** [[LiaS]]-[[LiaR]]
  
* '''Localization:''' cytoplasm (according to Swiss-Prot)
+
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 21:14, 21 November 2011

Gene name liaR
Synonyms yvqC
Essential no
Product two-component response regulator
Function regulation of the liaI-liaH-liaG-liaF-liaS-liaR

operon in response to bacitracin

Interactions involving this protein in SubtInteract: LiaR
MW, pI 22 kDa, 4.956
Gene length, protein length 633 bp, 211 aa
Immediate neighbours gerAC, liaS
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvqC context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

transcription factors and their control, resistance against oxidative and electrophile stress, resistance against toxins/ antibiotics, phosphoproteins

This gene is a member of the following regulons

LiaR regulon

The LiaR regulon

The gene

Basic information

  • Locus tag: BSU33080

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: regulation of the liaI-liaH-liaG-liaF-liaS-liaR operon in response to bacitracin
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on a Asp residue by LiaS
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage


Your additional remarks

References

Additional publications: PubMed

Diana Wolf, Falk Kalamorz, Tina Wecke, Anna Juszczak, Ulrike Mäder, Georg Homuth, Sina Jordan, Janine Kirstein, Michael Hoppert, Birgit Voigt, Michael Hecker, Thorsten Mascher
In-depth profiling of the LiaR response of Bacillus subtilis.
J Bacteriol: 2010, 192(18);4680-93
[PubMed:20639339] [WorldCat.org] [DOI] (I p)

Andriansjah Rukmana, Takuya Morimoto, Hiroki Takahashi, Giyanto, Naotake Ogasawara
Assessment of transcriptional responses of Bacillus subtilis cells to the antibiotic enduracidin, which interferes with cell wall synthesis, using a high-density tiling chip.
Genes Genet Syst: 2009, 84(4);253-67
[PubMed:20057163] [WorldCat.org] [DOI] (P p)

Tina Wecke, Daniela Zühlke, Ulrike Mäder, Sina Jordan, Birgit Voigt, Stefan Pelzer, Harald Labischinski, Georg Homuth, Michael Hecker, Thorsten Mascher
Daptomycin versus Friulimicin B: in-depth profiling of Bacillus subtilis cell envelope stress responses.
Antimicrob Agents Chemother: 2009, 53(4);1619-23
[PubMed:19164157] [WorldCat.org] [DOI] (I p)

Anna-Barbara Hachmann, Esther R Angert, John D Helmann
Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin.
Antimicrob Agents Chemother: 2009, 53(4);1598-609
[PubMed:19164152] [WorldCat.org] [DOI] (I p)

Eva Rietkötter, Diana Hoyer, Thorsten Mascher
Bacitracin sensing in Bacillus subtilis.
Mol Microbiol: 2008, 68(3);768-85
[PubMed:18394148] [WorldCat.org] [DOI] (I p)

Bronwyn G Butcher, Yi-Pin Lin, John D Helmann
The yydFGHIJ operon of Bacillus subtilis encodes a peptide that induces the LiaRS two-component system.
J Bacteriol: 2007, 189(23);8616-25
[PubMed:17921301] [WorldCat.org] [DOI] (I p)

Sina Jordan, Eva Rietkötter, Mark A Strauch, Falk Kalamorz, Bronwyn G Butcher, John D Helmann, Thorsten Mascher
LiaRS-dependent gene expression is embedded in transition state regulation in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 8);2530-2540
[PubMed:17660417] [WorldCat.org] [DOI] (P p)

Hanne-Leena Hyyryläinen, Milla Pietiäinen, Tuula Lundén, Anna Ekman, Marika Gardemeister, Sanna Murtomäki-Repo, Haike Antelmann, Michael Hecker, Leena Valmu, Matti Sarvas, Vesa P Kontinen
The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 7);2126-2136
[PubMed:17600057] [WorldCat.org] [DOI] (P p)

Sina Jordan, Anja Junker, John D Helmann, Thorsten Mascher
Regulation of LiaRS-dependent gene expression in bacillus subtilis: identification of inhibitor proteins, regulator binding sites, and target genes of a conserved cell envelope stress-sensing two-component system.
J Bacteriol: 2006, 188(14);5153-66
[PubMed:16816187] [WorldCat.org] [DOI] (P p)

Thorsten Mascher, Sara L Zimmer, Terry-Ann Smith, John D Helmann
Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis.
Antimicrob Agents Chemother: 2004, 48(8);2888-96
[PubMed:15273097] [WorldCat.org] [DOI] (P p)

Mélanie A Hamon, Nicola R Stanley, Robert A Britton, Alan D Grossman, Beth A Lazazzera
Identification of AbrB-regulated genes involved in biofilm formation by Bacillus subtilis.
Mol Microbiol: 2004, 52(3);847-60
[PubMed:15101989] [WorldCat.org] [DOI] (P p)

Thorsten Mascher, Neil G Margulis, Tao Wang, Rick W Ye, John D Helmann
Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon.
Mol Microbiol: 2003, 50(5);1591-604
[PubMed:14651641] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)