FloT

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU31010

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • SigW-dependent expression of fabF and the yuaF-floT-yuaI operon result in reduced membrane fluidity PubMed
  • recruits YuaF to focal assemblies PubMed
  • controls protease activity of FtsH PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • forms homo-oligomers PubMed
  • YuaF-FloT PubMed
  • FloT-FtsH PubMed
  • FloT-FloA PubMed
  • FloT-SecY PubMed
  • FloT-FtsX PubMed
  • FloT-OppA PubMed
  • FloT-SdhA PubMed

• Localization:
  • membrane associated PubMed
  • co-localizes with FloA and KinC in discrete foci membrane PubMed
  • forms discrete focal structures in the cytoplasma membrane PubMed

Database entries

• BsubCyc: BSU31010

• Structure:

• UniProt: O32076

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: yuaF-floT-yuaI PubMed

• Expression browser: floT PubMed

• Sigma factor: SigW PubMed

• 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:

• two-hybrid system:

• Antibody:

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

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)