OpuAC

• Description: glycine betaine ABC transporter (binding protein)
  
  

Gene name	opuAC
Synonyms
Essential	no
Product	glycine betaine ABC transporter (binding protein)
Function	compatible solute transport
Gene expression levels in SubtiExpress: opuAC
Interactions involving this protein in SubtInteract: OpuAC
Metabolic function and regulation of this protein in SubtiPathways: opuAC
MW, pI	32 kDa, 8.015
Gene length, protein length	879 bp, 293 aa
Immediate neighbours	opuAB, amhX
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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: BSU03000

Database entries

• BsubCyc: BSU03000

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • binding for subsequent uptake of glycine betaine PubMed
  • binding for subsequent uptake of dimethylglycine PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:
  • K_D for glycine betaine: 26 µM PubMed
  • K_D for dimethylglycine: 172 µM PubMed

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • OpuAA-OpuAB-OpuAC PubMed

• Localization: associated to the membrane (via OpuAB) PubMed

Database entries

• BsubCyc: BSU03000

• Structure: 2B4L (complex with glycine betaine), 3CHG (in complex with DMSA)

• UniProt: P46922

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: opuAA-opuAB-opuAC PubMed

• Expression browser: opuAC PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by osmotic stress PubMed
  • repressed by intracellular glycine betaine PubMed

• Regulatory mechanism:
  • RemA: transcription activation PubMed

• 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

References

Abdallah Bashir, Tamara Hoffmann, Sander H J Smits, Erhard Bremer
Dimethylglycine provides salt and temperature stress protection to Bacillus subtilis.
Appl Environ Microbiol: 2014, 80(9);2773-85
[PubMed:24561588] [WorldCat.org] [DOI] (I p)

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)

Sander H J Smits, Marina Höing, Justin Lecher, Mohamed Jebbar, Lutz Schmitt, Erhard Bremer
The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies.
J Bacteriol: 2008, 190(16);5663-71
[PubMed:18567662] [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, Linda Sohn-Bösser, Jason Breed, Wolfram Welte, Lutz Schmitt, Erhard Bremer
Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine.
J Mol Biol: 2006, 357(2);592-606
[PubMed:16445940] [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, J Gade, E Bremer
Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant.
J Bacteriol: 1997, 179(20);6213-20
[PubMed:9335265] [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)