Difference between revisions of "FliY"

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(Expression and regulation)
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* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
 +
** [[FlhG]]-([[FliY]]-[[FliM]])-[[FliG]] {{PubMed|25733861}}
  
 
* '''[[Localization]]:''' cell membrane (according to Swiss-Prot)
 
* '''[[Localization]]:''' cell membrane (according to Swiss-Prot)
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=References=
 
=References=
  
<pubmed>14749334,1447979,,14651647, 9657996,8157612,15175317,12920116 17850253 22517742 24386445</pubmed>
+
<pubmed>14749334,1447979,25733861,14651647, 9657996,8157612,15175317,12920116 17850253 22517742 24386445</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:38, 4 March 2015

  • Description: flagellar motor switch protein

Gene name fliY
Synonyms cheD
Essential no
Product flagellar motor switch 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