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Literature summary extracted from

  • Horn, C.; Jenewein, S.; Sohn-Boesser, L.; Bremer, E.; Schmitt, L.
    Biochemical and structural analysis of the Bacillus subtilis ABC transporter OpuA and its isolated subunits (2005), J. Mol. Microbiol. Biotechnol., 10, 76-91.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.6.2.9 additional information nucleotide-binding protein domain not stimulated by glycine betaine Bacillus subtilis
7.6.2.9 negatively charged lipid
-
Lactococcus lactis
7.6.2.9 phosphate ion-containing buffer
-
Lactococcus lactis

Application

EC Number Application Comment Organism
7.6.2.9 additional information osmotic control of the OpuA operon allows the cell to sensitively adjust the number of the OpuA transporter to the physiological need of the cell Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.6.2.9 nucleotide-binding protein domain cloned as an N- or C-terminal His-tagged fusion protein and overexpressed in Escherichia coli BL21 (DE3) under the control of an arabinose-inducible promoter, overexpression of the transmembrane domain only possible in Walker strains BL21(DE3)C41 and C43 under the control of an ITPG- or arabinose-inducible promoter as N- and C-terminal His- and Strep-tagged versions Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.6.2.9 substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
7.6.2.9 additional information deletion of the various Opu transport systems prevents thermoprotection by compatible solutes Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.9 cytosol nucleotide-binding domain of the enzyme Bacillus subtilis 5829
-
7.6.2.9 membrane transmembrane domain Bacillus subtilis 16020
-
7.6.2.9 membrane transmembrane domain fused to the substrate-binding domain Lactococcus lactis 16020
-
7.6.2.9 periplasm substrate-binding protein domain Bacillus subtilis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.6.2.9 K+ K+ binding site within the nucleotide-binding protein domain, stimulation of the nucleotide-binding protein domain 4fold higher than with Na+ Bacillus subtilis
7.6.2.9 Mg2+ essential for effective binding Bacillus subtilis
7.6.2.9 Na+ stimulation of the nucleotide-binding protein domain 4fold lower than with K+ Bacillus subtilis

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.9 by affinity tag as first step and gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.9 ATP + H2O + glycine betaine/out
-
Bacillus subtilis ADP + phosphate + glycine betaine/in
-
?
7.6.2.9 ATP + H2O + proline betaine/out
-
Bacillus subtilis ADP + phosphate + proline betaine/in
-
?

Subunits

EC Number Subunits Comment Organism
7.6.2.9 dimer nucleotide-binding protein domain, displays lower ATPase activity than the dimeric form Bacillus subtilis
7.6.2.9 monomer nucleotide-binding protein domain, displays higher ATPase activity than the dimeric form Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
7.6.2.9 OpuA
-
Bacillus subtilis
7.6.2.9 OpuA
-
Lactococcus lactis