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Literature summary for 7.6.2.9 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
Search for more literature for 7.6.2.9

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 OpuB and OpuC
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Subunits

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

Synonyms

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