Literature summary for 7.6.2.9 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.

Activating Compound

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

Application

Application	Comment	Organism
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)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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)

Crystallization (Comment)	Organism
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

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

Localization

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-
Lactococcus lactis	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
OpuA	-	Bacillus subtilis
OpuA	-	Lactococcus lactis