Difference between revisions of "FloT"

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** a ''[[floT]] [[floA]]'' double mutant has a strong synthetic defect in motility, cell morphology, and transformation efficiency {{PubMed|22753055}}
 
** a ''[[floT]] [[floA]]'' double mutant has a strong synthetic defect in motility, cell morphology, and transformation efficiency {{PubMed|22753055}}
 
** a ''[[floT]] [[floA]]'' double mutant has a [[sporulation]] defect, due to the lack of [[FtsH]] {{PubMed|22882210}}
 
** a ''[[floT]] [[floA]]'' double mutant has a [[sporulation]] defect, due to the lack of [[FtsH]] {{PubMed|22882210}}
 +
** a ''[[floT]]'' mutant displays a defective growth under oxygen-limiting conditions {{PubMed|25909364}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
 
** forms homo-oligomers {{PubMed|23651456}}
 
** forms homo-oligomers {{PubMed|23651456}}
 +
** oligomerization depends on the glutamate-alanine repeats {{PubMed|25909364}}
 
** [[YuaF]]-[[FloT]] {{PubMed|22753055}}
 
** [[YuaF]]-[[FloT]] {{PubMed|22753055}}
 
** [[FloT]]-[[FtsH]] {{PubMed|22882210}}
 
** [[FloT]]-[[FtsH]] {{PubMed|22882210}}
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** [[FloT]]-[[OppA]] {{PubMed|23651456}}
 
** [[FloT]]-[[OppA]] {{PubMed|23651456}}
 
** [[FloT]]-[[SdhA]] {{PubMed|23651456}}
 
** [[FloT]]-[[SdhA]] {{PubMed|23651456}}
 +
** [[FloT]]-[[ResE]] {{PubMed|25909364}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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** co-localizes with [[FloA]] and [[KinC]] in discrete foci membrane {{PubMed|20713508}}
 
** co-localizes with [[FloA]] and [[KinC]] in discrete foci membrane {{PubMed|20713508}}
 
** forms discrete focal structures in the cytoplasma membrane {{PubMed|22753055}}
 
** forms discrete focal structures in the cytoplasma membrane {{PubMed|22753055}}
 +
** 6 foci [[FloT]] of are detected in strain 3610 {{PubMed|25909364}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Mutant:'''
 
* '''Mutant:'''
 +
** JS152 (markerless), available in [[Daniel Lopez]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
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* '''GFP fusion:'''
 
* '''GFP fusion:'''
 +
** GK38 (168 [[amyE]]::P[[floT-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:'''  
+
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Daniel Lopez]]'s lab
  
 
* '''Antibody:'''
 
* '''Antibody:'''

Revision as of 11:35, 30 April 2015

  • 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

Gene name floT
Synonyms yuaG, yuaH
Essential no
Product bacterial flotillin-like 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:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Daniel Lopez's lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

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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