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Literature summary for 7.6.2.9 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
Search for more literature for 7.6.2.9

Cloned(Commentary)

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

Protein Variants

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

General Stability

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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)

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

Subunits

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

Turnover Number [1/s]

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