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Literature summary extracted from

  • Horn, C.; Bremer, E.; Schmitt, L.
    Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis (2003), J. Mol. Biol., 334, 403-419.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.6.2.9 expression of OpuAA protein in Escherichia coli Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
7.6.2.9 E171Q the monomer is the preferred species for the nucleotide-free state in solution Bacillus subtilis

General Stability

EC Number General Stability Organism
7.6.2.9 both monomeric and dimeric OpuA species are stabilized at 1 M NaCl Bacillus subtilis
7.6.2.9 OpuAA forms a stable dimer in the nucleotide-free state in solution Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.6.2.9 0.25
-
 ATP 22ºC, pH 8.0, 0.15 M NaCl, monomeric and dimeric OpuAA Bacillus subtilis
7.6.2.9 0.45
-
 ATP 22ºC, pH 8.0, 1 M NaCl, monomeric OpuAA Bacillus subtilis
7.6.2.9 1.3
-
 ATP 22ºC, pH 8.0, 1 M NaCl, dimeric OpuAA Bacillus subtilis
7.6.2.9 5.4
-
 ATP 22ºC, pH 8.0, 1 M KCl, monomeric OpuAA Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.9 cytosol OpuAA, a nucleotide binding protein of the OpuA transporter Bacillus subtilis 5829
-
7.6.2.9 membrane
-
 Bacillus subtilis 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.6.2.9 47700
-
 OpuAA monomer, calculated from cDNA Bacillus subtilis
7.6.2.9 65000
-
 OpuAA, gel filtration Bacillus subtilis
7.6.2.9 95400
-
 OpuAA dimer, calculated from cDNA Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.9 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.9 OpuAA, purified to homogeneity, affinity chromatography and gel filtration Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
7.6.2.9 ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] OpuA is an osmoprotectant uptake system which imports glycine and betaine. It consists of three components, the ATPase OpuAA, the integral membrane protein OpuAB and the extracellular substrate binding domain OpuAC. The ABC transporter couples ATP hydrolysis with substrate translocation across the membrane in a vectorial manner Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.9 ADP + H2O OpuAA protein, ATPase activity Bacillus subtilis AMP + phosphate
-
 ?
7.6.2.9 AMP + H2O OpuAA protein, ATPase activity, similar substrate affinities to monomeric and dimeric states Bacillus subtilis adenine + phosphate
-
 ?
7.6.2.9 ATP + H2O OpuAA protein, ATPase activity Bacillus subtilis ADP + phosphate
-
 ?
7.6.2.9 ATP + H2O + betaine/out
-
 Bacillus subtilis ADP + phosphate + betaine/in
-
 ?

Subunits

EC Number Subunits Comment Organism
7.6.2.9 monomer 1 * 65000, gel filtration Bacillus subtilis
7.6.2.9 More a peak of 150000 corresponds to dimeric OpuAA Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.6.2.9 0.004
-
 ATP 22ºC, pH 8.0, 0.15 M NaCl, monomeric and dimeric OpuAA Bacillus subtilis
7.6.2.9 0.004
-
 ATP 22ºC, pH 8.0, 1 M NaCl, dimeric OpuAA Bacillus subtilis
7.6.2.9 0.038
-
 ATP 22ºC, pH 8.0, 1 M NaCl, monomeric OpuAA Bacillus subtilis
7.6.2.9 0.25
-
 ATP 22ºC, pH 8.0, 1 M KCl, monomeric OpuAA Bacillus subtilis