LiaF

• Description: negative effector of LiaR
  
  

Gene name	liaF
Synonyms	yvqF
Essential	no
Product	negative effector of LiaR
Function	control of LiaR activity
MW, pI	26 kDa, 9.211
Gene length, protein length	723 bp, 241 aa
Immediate neighbours	liaS, liaG
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, resistance against oxidative and electrophile stress, resistance against toxins/ antibiotics, membrane proteins

This gene is a member of the following regulons

LiaR regulon

The gene

Basic information

• Locus tag: BSU33100

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • cell membrane (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: O32199

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • liaI-liaH-liaG-liaF-liaS-liaR PubMed
  • liaG-liaF-liaS-liaR PubMed

• Expression browser: liaF PubMed

• Sigma factor:
  • liaI: SigA PubMed
  • liaG: SigA PubMed

• Regulation:
  • liaI: induced by bacitracin and rhamnolipids (LiaR) PubMed
  • liaI: repressed during logarithmic growth (AbrB) PubMed, indirect regulation by AbrB PubMed
  • liaG: constitutive

• Regulatory mechanism:
  • LiaR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)

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)

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)

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)