Difference between revisions of "OpuAB"

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= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
 
+
{{SubtiWiki regulon|[[RemA regulon]]}}
  
 
=The gene=
 
=The gene=
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* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[RemA]]: transcription activation {{PubMed|23646920}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
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=References=
 
=References=
  
<pubmed>16645306,16225868,7622480,10092453,18763711 7622480 16225868, 21296969 22383849 23175650</pubmed>
+
<pubmed>16645306,16225868,7622480,10092453,18763711 7622480 16225868, 21296969 22383849 23175650 23646920</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:12, 24 May 2013

Gene name opuAB
Synonyms
Essential no
Product glycine betaine ABC transporter (permease)
Function compatible solute transport
Gene expression levels in SubtiExpress: opuAB
Interactions involving this protein in SubtInteract: OpuAB
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 30 kDa, 9.837
Gene length, protein length 846 bp, 282 aa
Immediate neighbours opuAA, opuAC
Sequences Protein DNA DNA_with_flanks
Genetic context
OpuAB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
OpuAB expression.png















Categories containing this gene/protein

ABC transporters, coping with hyper-osmotic stress, membrane proteins

This gene is a member of the following regulons

RemA regulon

The gene

Basic information

  • Locus tag: BSU02990

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: ABC transmembrane type-1 domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • induced by osmotic stress PubMed
    • repressed by intracellular glycine betaine PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Erhard Bremer, University of Marburg, Germany homepage

Your additional remarks

References

Jared T Winkelman, Anna C Bree, Ashley R Bate, Patrick Eichenberger, Richard L Gourse, Daniel B Kearns
RemA is a DNA-binding protein that activates biofilm matrix gene expression in Bacillus subtilis.
Mol Microbiol: 2013, 88(5);984-97
[PubMed:23646920] [WorldCat.org] [DOI] (I p)

Tamara Hoffmann, Annette Wensing, Margot Brosius, Leif Steil, Uwe Völker, Erhard Bremer
Osmotic control of opuA expression in Bacillus subtilis and its modulation in response to intracellular glycine betaine and proline pools.
J Bacteriol: 2013, 195(3);510-22
[PubMed:23175650] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Tamara Hoffmann, Erhard Bremer
Protection of Bacillus subtilis against cold stress via compatible-solute acquisition.
J Bacteriol: 2011, 193(7);1552-62
[PubMed:21296969] [WorldCat.org] [DOI] (I 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)

Carsten Horn, Stefan Jenewein, Linda Sohn-Bösser, Erhard Bremer, Lutz Schmitt
Biochemical and structural analysis of the Bacillus subtilis ABC transporter OpuA and its isolated subunits.
J Mol Microbiol Biotechnol: 2005, 10(2-4);76-91
[PubMed:16645306] [WorldCat.org] [DOI] (P p)

Carsten Horn, Erhard Bremer, Lutz Schmitt
Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis.
FEBS Lett: 2005, 579(25);5765-8
[PubMed:16225868] [WorldCat.org] [DOI] (P p)

Y Quentin, G Fichant, F Denizot
Inventory, assembly and analysis of Bacillus subtilis ABC transport systems.
J Mol Biol: 1999, 287(3);467-84
[PubMed:10092453] [WorldCat.org] [DOI] (P p)

B Kempf, E Bremer
OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis.
J Biol Chem: 1995, 270(28);16701-13
[PubMed:7622480] [WorldCat.org] [DOI] (P p)