Difference between revisions of "FliY"

From SubtiWiki
Jump to: navigation, search
Line 1: Line 1:
* '''Description:''' flagellar motor switch protein <br/><br/>
+
* '''Description:''' flagellar C ring protein <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
Line 10: Line 10:
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || flagellar motor switch protein
+
|style="background:#ABCDEF;" align="center"| '''Product''' || flagellar C ring protein
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || movement and chemotaxis  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || movement and chemotaxis  

Revision as of 12:18, 4 March 2015

  • Description: flagellar C ring protein

Gene name fliY
Synonyms cheD
Essential no
Product flagellar C ring protein
Function movement and chemotaxis
Gene expression levels in SubtiExpress: fliY
MW, pI 40 kDa, 4.117
Gene length, protein length 1134 bp, 378 aa
Immediate neighbours fliM, cheY
Sequences Protein DNA DNA_with_flanks
Genetic context
FliY context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FliY expression.png















Categories containing this gene/protein

motility and chemotaxis, membrane proteins, phosphoproteins

This gene is a member of the following regulons

CodY regulon, DegU regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16320

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: fliN/mopA/spaO family (according to Swiss-Prot) cheC family

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-251 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

Additional information

Expression and regulation

  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1488 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1885 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 850 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 900 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 713 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Jan S Schuhmacher, Florian Rossmann, Felix Dempwolff, Carina Knauer, Florian Altegoer, Wieland Steinchen, Anja K Dörrich, Andreas Klingl, Milena Stephan, Uwe Linne, Kai M Thormann, Gert Bange
MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.
Proc Natl Acad Sci U S A: 2015, 112(10);3092-7
[PubMed:25733861] [WorldCat.org] [DOI] (I p)

Serena Mordini, Cecilia Osera, Simone Marini, Francesco Scavone, Riccardo Bellazzi, Alessandro Galizzi, Cinzia Calvio
The role of SwrA, DegU and P(D3) in fla/che expression in B. subtilis.
PLoS One: 2013, 8(12);e85065
[PubMed:24386445] [WorldCat.org] [DOI] (I e)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi
Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2007, 66(2);395-409
[PubMed:17850253] [WorldCat.org] [DOI] (P p)

H Werhane, P Lopez, M Mendel, M Zimmer, G W Ordal, L M Márquez-Magaña
The last gene of the fla/che operon in Bacillus subtilis, ylxL, is required for maximal sigmaD function.
J Bacteriol: 2004, 186(12);4025-9
[PubMed:15175317] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Travis J Muff, George W Ordal
Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade.
J Biol Chem: 2004, 279(21);21787-92
[PubMed:14749334] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Michael W Bunn, Vincent J Cannistraro, George W Ordal
Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch.
J Biol Chem: 2003, 278(49);48611-6
[PubMed:12920116] [WorldCat.org] [DOI] (P p)

W Estacio, S S Anna-Arriola, M Adedipe, L M Márquez-Magaña
Dual promoters are responsible for transcription initiation of the fla/che operon in Bacillus subtilis.
J Bacteriol: 1998, 180(14);3548-55
[PubMed:9657996] [WorldCat.org] [DOI] (P p)

L M Márquez-Magaña, M J Chamberlin
Characterization of the sigD transcription unit of Bacillus subtilis.
J Bacteriol: 1994, 176(8);2427-34
[PubMed:8157612] [WorldCat.org] [DOI] (P p)

D S Bischoff, G W Ordal
Identification and characterization of FliY, a novel component of the Bacillus subtilis flagellar switch complex.
Mol Microbiol: 1992, 6(18);2715-23
[PubMed:1447979] [WorldCat.org] [DOI] (P p)