Difference between revisions of "RibU"

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=== Additional information===
 
=== Additional information===
 
  
 
=The protein=
 
=The protein=
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<pubmed> 20497229 22574898 24362466 </pubmed>
 
<pubmed> 20497229 22574898 24362466 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>12456892, 20972419,17693491,21815947  </pubmed>
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<pubmed>12456892, 20972419,17693491,21815947  24356467 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:30, 16 January 2014

Gene name ribU
Synonyms ypaA
Essential no
Product S protein of riboflavin ECF transporter
Function riboflavin uptake
Gene expression levels in SubtiExpress: ribU
Interactions involving this protein in SubtInteract: RibU
Metabolic function and regulation of this protein in SubtiPathways:
ribU
MW, pI 20 kDa, 10.12
Gene length, protein length 570 bp, 190 aa
Immediate neighbours fer, ypzE
Sequences Protein DNA DNA_with_flanks
Genetic context
YpaA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
500px















Categories containing this gene/protein

ECF transporter, biosynthesis of cofactors, membrane proteins

This gene is a member of the following regulons

FMN-box

The gene

Basic information

  • Locus tag: BSU23050

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 3P5N (RibU from Staphylococcus aureus)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Dirk J Slotboom
Structural and mechanistic insights into prokaryotic energy-coupling factor transporters.
Nat Rev Microbiol: 2014, 12(2);79-87
[PubMed:24362466] [WorldCat.org] [DOI] (I p)

Guus B Erkens, Maria Majsnerowska, Josy ter Beek, Dirk Jan Slotboom
Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes.
Biochemistry: 2012, 51(22);4390-6
[PubMed:22574898] [WorldCat.org] [DOI] (I p)

Thomas Eitinger, Dmitry A Rodionov, Mathias Grote, Erwin Schneider
Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
FEMS Microbiol Rev: 2011, 35(1);3-67
[PubMed:20497229] [WorldCat.org] [DOI] (I p)

Original publications

Jianing Song, Changge Ji, John Z H Zhang
Unveiling the gating mechanism of ECF transporter RibU.
Sci Rep: 2013, 3;3566
[PubMed:24356467] [WorldCat.org] [DOI] (I e)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Peng Zhang, Jiawei Wang, Yigong Shi
Structure and mechanism of the S component of a bacterial ECF transporter.
Nature: 2010, 468(7324);717-20
[PubMed:20972419] [WorldCat.org] [DOI] (I p)

Christian Vogl, Simon Grill, Oliver Schilling, Jörg Stülke, Matthias Mack, Jürgen Stolz
Characterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum.
J Bacteriol: 2007, 189(20);7367-75
[PubMed:17693491] [WorldCat.org] [DOI] (P p)

Wade C Winkler, Smadar Cohen-Chalamish, Ronald R Breaker
An mRNA structure that controls gene expression by binding FMN.
Proc Natl Acad Sci U S A: 2002, 99(25);15908-13
[PubMed:12456892] [WorldCat.org] [DOI] (P p)