Difference between revisions of "LiaI"

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* '''Description:''' resistance against oxidative stress and cell wall antibiotics, may act as membrane anchor for [[LiaH]] <br/><br/>
+
* '''Description:''' resistance against oxidative stress and cell wall antibiotics, membrane anchor for [[LiaH]] <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || unknown
+
|style="background:#ABCDEF;" align="center"| '''Product''' || membrane anchor for [[LiaH]] 
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || resistance against oxidative stress and cell wall antibiotics
 
|style="background:#ABCDEF;" align="center"|'''Function''' || resistance against oxidative stress and cell wall antibiotics
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 +
** [[LiaI]]-[[LiaH]] {{PubMed|24666271}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
** cell membrane (according to Swiss-Prot)
+
** cell membrane {{PubMed|24666271}}
 +
** forms highly dynamic membrane-associated foci under non-inducing conditions {{PubMed|24666271}}
 +
** co-localizes with [[LiaH]] in distinct static spots at the cytoplasma membrane under stress conditions {{PubMed|24666271}}
  
 
=== Database entries ===
 
=== Database entries ===
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=References=
 
=References=
<pubmed>19164152,15273097,17660417,17600057,20057163 ,16816187,15101989,17660417,12850135 16816187, 20639339 20817675 ,22092710</pubmed>
+
<pubmed>19164152,15273097,17660417,17600057,20057163 ,16816187,15101989,17660417,12850135 16816187, 20639339 20817675 ,22092710 24666271 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:09, 10 October 2014

  • Description: resistance against oxidative stress and cell wall antibiotics, membrane anchor for LiaH

Gene name liaI
Synonyms yvqI
Essential no
Product membrane anchor for LiaH
Function resistance against oxidative stress and cell wall antibiotics
Gene expression levels in SubtiExpress: liaI
MW, pI 13 kDa, 9.303
Gene length, protein length 378 bp, 126 aa
Immediate neighbours liaH, yvqJ
Sequences Protein DNA DNA_with_flanks
Genetic context
YvqI context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LiaI expression.png















Categories containing this gene/protein

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: BSU33130

Phenotypes of a mutant

Database entries

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

Additional information

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:
  • Localization:
    • cell membrane PubMed
    • forms highly dynamic membrane-associated foci under non-inducing conditions PubMed
    • co-localizes with LiaH in distinct static spots at the cytoplasma membrane under stress conditions PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Julia Domínguez-Escobar, Diana Wolf, Georg Fritz, Carolin Höfler, Roland Wedlich-Söldner, Thorsten Mascher
Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis.
Mol Microbiol: 2014, 92(4);716-32
[PubMed:24666271] [WorldCat.org] [DOI] (I p)

Tina Wecke, Tobias Bauer, Henning Harth, Ulrike Mäder, Thorsten Mascher
The rhamnolipid stress response of Bacillus subtilis.
FEMS Microbiol Lett: 2011, 323(2);113-23
[PubMed:22092710] [WorldCat.org] [DOI] (I p)

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

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)

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)

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)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)