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
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	32 kDa, 8.015
Gene length, protein length	879 bp, 293 aa
Immediate neighbours	opuAB, amhX
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU03000

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cell membrane (according to Swiss-Prot)

Database entries

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

• Swiss prot entry: P46922

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• 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

References

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)

1. Smits SH, Höing M, Lecher J, Jebbar M, Schmitt L, Bremer E. (2008) The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies. J Bacteriol. Aug;190(16): 5663-71. PubMed
2. Kempf B, Bremer E. (1995) OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J Biol Chem. Jul 14;270(28): 16701-13. PubMed
3. Horn C, Bremer E, Schmitt L. (2005) Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis. FEBS Lett. Oct 24;579(25): 5765-8. PubMed
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed