SubtiBank SubtiBank
liaS [2019-06-06 09:45:03]
You are currently viewing an outdated version of SubtiWiki. Please use the newest version!

liaS [2019-06-06 09:45:03]

two-component sensor kinase/phosphatase, response to bacitracin
Locus
BSU33090
Isoelectric point
7.33
Molecular weight
40.55 kDa
Protein length
360 aa Sequence Blast
Gene length
1083 bp Sequence Blast
Function
control of LiaR activity in response to bacitracin
Product
two-component sensor kinase
Essential
no
Synonyms
yvqE

Genomic Context

      
Loading

Categories containing this gene/protein

Gene

Coordinates
3,395,035 3,396,117

The protein

Catalyzed reaction/ biological activity

  • autophosphorylation, phosphorylation of LiaR
  • dephosphorylation of LiaR in the absence of the stress signal PubMed
  • Domains

  • two transmembrane segments, C-terminal histidine phosphotransferase domain
  • Modification

  • autophosphorylation on a His residue
  • Effectors of protein activity

  • LiaS kinase activity is inhibited by LiaF, phosphatase acitivity is maintained by LiaF in the absence of the stress signal PubMed
  • Structure

  • 3GIG (DesK, corresponds to the C-terminal domain, aa 149 ... 343, 25% identity) PubMed
  • Localization

  • cell membrane (according to Swiss-Prot)
  • Expression and Regulation

    Operons

    Description

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon
  • Regulatory mechanism

  • LiaR: activation, PubMed, in LiaR regulon
  • Regulation

  • liaG: constitutive
  • view in new tab

    Description

    Regulation

  • liaG: constitutive
  • view in new tab

    Biological materials

    Mutant

  • MGNA-B036 (yvqE::erm), available at the NBRP B. subtilis, Japan
  • BKE33090 (liaS::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_GAGGCTGGCAAGCATTTTTT, downstream forward: _UP4_CCGGAAGAAAAAGGAGAGAA
  • BKK33090 (liaS::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_GAGGCTGGCAAGCATTTTTT, downstream forward: _UP4_CCGGAAGAAAAAGGAGAGAA
  • Labs working on this gene/protein

  • John Helmann, Cornell University, USA Homepage
  • References

    Reviews

    Loading

    Original publications

    Loading