Difference between revisions of "FloT"

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* '''Description:''' similar to flotillin 1, orchestration of physiological processes in lipid microdomains, involved in the control of membrane fluidity, confers (together with [[YuaF]]) resistance to cefuroxime  <br/><br/>
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* '''Description:''' membrane-associated scaffold protein, orchestration of physiological processes in lipid microdomains, involved in the control of membrane fluidity, confers (together with [[YuaF]]) resistance to cefuroxime  <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  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"| '''Product''' ||  bacterial flotillin-like protein
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|style="background:#ABCDEF;" align="center"| '''Product''' ||  membrane-associated scaffold protein
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || involved in the control of membrane fluidity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || involved in the control of membrane fluidity
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** oligomerization depends on the glutamate-alanine repeats {{PubMed|25909364}}
 
** oligomerization depends on the glutamate-alanine repeats {{PubMed|25909364}}
 
** [[YuaF]]-[[FloT]] {{PubMed|22753055}}
 
** [[YuaF]]-[[FloT]] {{PubMed|22753055}}
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** [[FloT]]-[[FtsH]] {{PubMed|22882210}}
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** [[FloT]]-[[FtsH]] {{PubMed|26297017,22882210}}
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** [[FloT]]-[[FloA]] {{PubMed|23651456}}
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** [[FloT]]-[[FloA]] {{PubMed|26297017,23651456}}
 
** [[FloT]]-[[SecY]] {{PubMed|23651456}}
 
** [[FloT]]-[[SecY]] {{PubMed|23651456}}
 
** [[FloT]]-[[FtsX]] {{PubMed|23651456}}
 
** [[FloT]]-[[FtsX]] {{PubMed|23651456}}
 
** [[FloT]]-[[OppA]] {{PubMed|23651456}}
 
** [[FloT]]-[[OppA]] {{PubMed|23651456}}
 
** [[FloT]]-[[SdhA]] {{PubMed|23651456}}
 
** [[FloT]]-[[SdhA]] {{PubMed|23651456}}
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** [[FloT]]-[[ResE]] {{PubMed|25909364}}
+
** [[FloT]]-[[ResE]] {{PubMed|26297017,25909364}}
 +
** [[FloT]]-[[KinC]] to stimulate KinC dimerization and activity {{PubMed|26297017}}
 +
** [[FloT]]-[[KinD]] {{PubMed|26297017}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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<pubmed> 25652542</pubmed>
 
<pubmed> 25652542</pubmed>
 
== Original publications ==
 
== Original publications ==
−
<pubmed>9987136,22753055, 12107147, 18763711, 19383680  20713508 23651456 22178969 ,23249255  22882210 25635948 25909364 24222488</pubmed>
+
<pubmed>9987136,22753055, 12107147, 18763711, 19383680  20713508 23651456 22178969 ,23249255  22882210 25635948 25909364 24222488 26297017</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:37, 28 August 2015

  • Description: membrane-associated scaffold protein, orchestration of physiological processes in lipid microdomains, involved in the control of membrane fluidity, confers (together with YuaF) resistance to cefuroxime

Gene name floT
Synonyms yuaG, yuaH
Essential no
Product membrane-associated scaffold protein
Function involved in the control of membrane fluidity
Gene expression levels in SubtiExpress: floT
Interactions involving this protein in SubtInteract: FloT
MW, pI 55 kDa, 5.135
Gene length, protein length 1527 bp, 509 aa
Immediate neighbours yuaI, yuaF
Sequences Protein DNA DNA_with_flanks
Genetic context
YuaG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FloT expression.png















Categories containing this gene/protein

biofilm formation, membrane dynamics, membrane proteins sporulation/ other, cell envelope stress proteins (controlled by SigM, V, W, X, Y)

This gene is a member of the following regulons

SigW regulon

The gene

Basic information

  • Locus tag: BSU31010

Phenotypes of a mutant

    • delayed onset of sporulation, reduced sporulation frequency
    • defect in motility PubMed
    • reduced protein secretion PubMed
    • a floT floA double mutant does not induce KinC-dependent biofilm formation upon addition of surfactin PubMed
    • a floT floA double mutant has a strong synthetic defect in motility, cell morphology, and transformation efficiency PubMed
    • a floT floA double mutant has a sporulation defect, due to the lack of FtsH PubMed
    • a floT mutant displays a defective growth under oxygen-limiting conditions PubMed

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:

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • expressed upon cell wall stress (SigW) PubMed
    • repressed by casamino acids PubMed
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1215 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 236 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
    • GK38 (168 amyE::PfloT-yfp (spc)), available in Daniel Lopez's lab
    • JS280 (3610 amyE::floT-gfp(spc)), available in Daniel Lopez's lab
    • JS153 (3610 lacA::floT-mEos2 (mls)), available in Daniel Lopez's lab
    • JS166 (3610 lacA::floT-PAmCherry (mls)), available in Daniel Lopez's lab
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH) for FloT PubMed, available in Daniel Lopez's lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Marc Bramkamp, Daniel Lopez
Exploring the existence of lipid rafts in bacteria.
Microbiol Mol Biol Rev: 2015, 79(1);81-100
[PubMed:25652542] [WorldCat.org] [DOI] (I p)

Original publications

Johannes Schneider, Benjamin Mielich-Süss, Richard Böhme, Daniel Lopez
In vivo characterization of the scaffold activity of flotillin on the membrane kinase KinC of Bacillus subtilis.
Microbiology (Reading): 2015, 161(9);1871-1887
[PubMed:26297017] [WorldCat.org] [DOI] (I p)

Johannes Schneider, Teresa Klein, Benjamin Mielich-Süss, Gudrun Koch, Christian Franke, Oscar P Kuipers, Ákos T Kovács, Markus Sauer, Daniel Lopez
Spatio-temporal remodeling of functional membrane microdomains organizes the signaling networks of a bacterium.
PLoS Genet: 2015, 11(4);e1005140
[PubMed:25909364] [WorldCat.org] [DOI] (I e)

Juri Niño Bach, Marc Bramkamp
Dissecting the molecular properties of prokaryotic flotillins.
PLoS One: 2015, 10(1);e0116750
[PubMed:25635948] [WorldCat.org] [DOI] (I e)

Benjamin Mielich-Süss, Johannes Schneider, Daniel Lopez
Overproduction of flotillin influences cell differentiation and shape in Bacillus subtilis.
mBio: 2013, 4(6);e00719-13
[PubMed:24222488] [WorldCat.org] [DOI] (I e)

Juri Niño Bach, Marc Bramkamp
Flotillins functionally organize the bacterial membrane.
Mol Microbiol: 2013, 88(6);1205-17
[PubMed:23651456] [WorldCat.org] [DOI] (I p)

Felix Dempwolff, Hanna M Wischhusen, Mara Specht, Peter L Graumann
The deletion of bacterial dynamin and flotillin genes results in pleiotrophic effects on cell division, cell growth and in cell shape maintenance.
BMC Microbiol: 2012, 12;298
[PubMed:23249255] [WorldCat.org] [DOI] (I e)

Ana Yepes, Johannes Schneider, Benjamin Mielich, Gudrun Koch, Juan-Carlos García-Betancur, Kumaran S Ramamurthi, Hera Vlamakis, Daniel López
The biofilm formation defect of a Bacillus subtilis flotillin-defective mutant involves the protease FtsH.
Mol Microbiol: 2012, 86(2);457-71
[PubMed:22882210] [WorldCat.org] [DOI] (I p)

Felix Dempwolff, Heiko M Möller, Peter L Graumann
Synthetic motility and cell shape defects associated with deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay of these proteins with NfeD proteins.
J Bacteriol: 2012, 194(17);4652-61
[PubMed:22753055] [WorldCat.org] [DOI] (I p)

Yong Heon Lee, Anthony W Kingston, John D Helmann
Glutamate dehydrogenase affects resistance to cell wall antibiotics in Bacillus subtilis.
J Bacteriol: 2012, 194(5);993-1001
[PubMed:22178969] [WorldCat.org] [DOI] (I p)

Daniel López, Roberto Kolter
Functional microdomains in bacterial membranes.
Genes Dev: 2010, 24(17);1893-902
[PubMed:20713508] [WorldCat.org] [DOI] (I p)

Catriona Donovan, Marc Bramkamp
Characterization and subcellular localization of a bacterial flotillin homologue.
Microbiology (Reading): 2009, 155(Pt 6);1786-1799
[PubMed:19383680] [WorldCat.org] [DOI] (P p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136] [WorldCat.org] [DOI] (P p)

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