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Literature summary extracted from

  • Kempf, B.; Gade, J.; Bremer, E.
    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 (1997), J. Bacteriol., 179, 6213-6220.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.9 Bacillus subtilis
-
 OpuB and OpuC
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
7.6.2.9 lipoprotein OpuA is a lipoprotein, the lipidless OpuAC-3 protein is held in the cytoplasmic membrane of Bacillus subtilis via its uncleaved hydrophobic signal peptide 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
-
 ?

Subunits

EC Number Subunits Comment Organism
7.6.2.9 More the transport system consists of an ATPase, OpuAA, an integral membrane protein OpuAB and a hydrophilic polypeptide OpuAC Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
7.6.2.9 OpuB opuB and opuC operons each encode a binding protein-dependent ABC transport system Bacillus subtilis
7.6.2.9 OpuC opuB and opuC operons each encode a binding protein-dependent ABC transport system Bacillus subtilis