Tue Dec 13 2016 11:16:35 GMT+0100 (CET)2025-05-14 11:20:24
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
membrane-associated scaffold protein, orchestration of physiological processes in lipid microdomains, involved in the control of membrane fluidity, confers (together with [[protein|YuaF]]) resistance to cefuroxime
locus
BSU31010
BSU_31010
function
involved in the control of membrane fluidity
control of membrane fluidity
ec
outlinks
bsu
BSU31010
BSU_31010
aminos
MTMPIIMIIGVVFFLLIALIAVFITKYRTAGPDEALIVTGSYLGNKNVHVDEGGNRIKIVRGGGTFVLPVFQQAEPLSLLSSKLDVSTPEVYTEQGVPVMADGTAIIKIGGSIGEIATAAEQFLGKSKDDREQEAREVLEGHLRSILGSMTVEEIYKNREKFSQEVQRVASQDLAKMGLVIVSFTIKDVRDKNGYLESLGKPRIAQVKRDADIATAEADKETRIKRAEADKDAKKSELERATEIAEAEKINQLKMAEFRREQDTAKANADQAYDLETARARQQVTEQEMQVKIIERQKQIELEEKEILRRERQYDSEVKKKADADRYSVEQSAAAEKAKQLAEADAKKYSIEAMAKAEAEKVRIDGLAKAEAEKAKGETEAEVIRLKGLAEAEAKEKIAAAFEQYGQAAIFDMIVKMLPEYAKQAAAPLSNIDKITVVDTGGSGESSGANKVTSYATNLMSSLQESLKASSGIDVKEMLENFSGKGNVKQSINELTNEIKEAKTIQKSE
[SW|Categories] containing this gene/protein
[SW|biofilm formation], [SW|membrane dynamics], [SW|membrane proteins], [SW|sporulation/ other], [SW|cell envelope stress proteins (controlled by SigM, V, W, X, Y)]
Gene
Coordinates on the chromosome (coding sequence)
3,180,465 -> 3,181,994
Gene
Phenotypes of a mutant
delayed onset of sporulation, reduced sporulation frequency
defect in motility [Pubmed|22753055]
reduced [SW|protein secretion] [Pubmed|23651456]
a ''[[protein|floT]] [[protein|floA]]'' double mutant does not induce [[protein|KinC]]-dependent biofilm formation upon addition of surfactin [Pubmed|20713508]
a ''[[protein|floT]] [[protein|floA]]'' double mutant has a strong synthetic defect in motility, cell morphology, and transformation efficiency [Pubmed|22753055]
a ''[[protein|floT]] [[protein|floA]]'' double mutant has a [SW|sporulation] defect, due to the lack of [[protein|FtsH]] [Pubmed|22882210]
a ''[[protein|floT]]'' mutant displays a defective growth under oxygen-limiting conditions [Pubmed|25909364]
delayed onset of sporulation, reduced sporulation frequency
defect in motility [Pubmed|22753055]
reduced [SW|protein secretion] [Pubmed|23651456]
a ''[[gene|floT]] [[gene|floA]]'' double mutant does not induce [[protein|KinC]]-dependent biofilm formation upon addition of surfactin [Pubmed|20713508]
a ''[[gene|floT]] [[gene|floA]]'' double mutant has a strong synthetic defect in motility, cell morphology, and transformation efficiency [Pubmed|22753055]
a ''[[gene|floT]] [[gene|floA]]'' double mutant has a [SW|sporulation] defect, due to the lack of [[protein|FtsH]] [Pubmed|22882210]
a ''[[gene|floT]]'' mutant displays a defective growth under oxygen-limiting conditions [Pubmed|25909364]
The protein
Catalyzed reaction/ biological activity
[[protein|SigW]]-dependent expression of ''[[protein|fabF]]'' and the ''[[protein|yuaF]]-[[protein|floT]]-[[protein|yuaI]]'' operon result in reduced membrane fluidity [Pubmed|21542858,22178969]
recruits [[protein|YuaF]] to focal assemblies [Pubmed|22753055]
controls protease activity of [[protein|FtsH]] [Pubmed|24222488]
[[protein|SigW]]-dependent expression of ''[[gene|fabF]]'' and the ''[[gene|yuaF]]-[[gene|floT]]-[[gene|yuaI]]'' operon result in reduced membrane fluidity [Pubmed|21542858,22178969]
recruits [[protein|YuaF]] to focal assemblies [Pubmed|22753055]
controls protease activity of [[protein|FtsH]] [Pubmed|24222488]
The protein
[SW|Interactions]
forms homo-oligomers [Pubmed|23651456]
oligomerization depends on the glutamate-alanine repeats [Pubmed|25909364]
[[protein|YuaF]]-[[protein|FloT]] [Pubmed|22753055]
[[protein|FloT]]-[[protein|FtsH]] [Pubmed|26297017,22882210]
[[protein|FloT]]-[[protein|FloA]] [Pubmed|26297017,23651456]
[[protein|FloT]]-[[protein|SecY]] [Pubmed|23651456]
[[protein|FloT]]-[[protein|FtsX]] [Pubmed|23651456]
[[protein|FloT]]-[[protein|OppA]] [Pubmed|23651456]
[[protein|FloT]]-[[protein|SdhA]] [Pubmed|23651456]
[[protein|FloT]]-[[protein|ResE]] [Pubmed|26297017,25909364]
[[protein|FloT]]-[[protein|KinC]] to stimulate [[protein|KinC]] dimerization and activity [Pubmed|26297017]
[[protein|FloT]]-[[protein|KinD]] [Pubmed|26297017]
Expression and Regulation
Operon
''[[protein|yuaF]]-[[protein|floT]]-[[protein|yuaI]]'' [Pubmed|9987136]
Expression and Regulation
[SW|Sigma factor]
[[protein|SigW]] [Pubmed|9987136]
Expression and Regulation
Regulation
expressed upon cell wall stress ([[protein|SigW]]) [Pubmed|9987136]
repressed by casamino acids [Pubmed|12107147]
Biological materials
Mutant
JS152 (markerless), available in [SW|Daniel Lopez]'s lab
MGNA-A213 (yuaG::erm), available at the [https://shigen.nig.ac.jp/bsub/resource/strainGeneDisrupted/detail/213 NBRP B. subtilis, Japan]
JS152 (markerless), available in [SW|Daniel Lopez]'s lab
BKE31010 ([[gene|floT]]::erm trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKE31010 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATATCAAATTCCTCCTTTT, downstream forward: _UP4_GAGTAAGGAAAGGGCAGAAC
BKK31010 ([[gene|floT]]::kan trpC2) available at [http://www.bgsc.org/getdetail.php?bgscid=BKK31010 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATATCAAATTCCTCCTTTT, downstream forward: _UP4_GAGTAAGGAAAGGGCAGAAC
References
Original publications
proteinLength
509
geneLength
1530
Gene
Coordinates
3,180,465 3,181,994
The protein
Paralogous protein(s)
[[this]]
Expression and Regulation
Operons
[[this]]
Expression and Regulation
Other regulations
[[this]]