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Literature summary extracted from

  • Eckford, P.D.; Sharom, F.J.
    The reconstituted Escherichia coli MsbA protein displays lipid flippase activity (2010), Biochem. J., 429, 195-203 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.5.2.6 gene msbA, overexpression of N-terminally His6-tagged enzyme in Escherichia coli Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.5.2.6 lipid A translocation of NBD-phosphatidylethanolamine is inhibited by the presence of the putative physiological substrate lipid A, probably due to competition for flipping of 7-nitrobenz-2-oxa-1,3-diazole-labeled phosphoethanolamine (NBD-PE) Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.5.2.6 membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.5.2.6 ATP + H2O + lipid A-core oligosaccharide[side 1] Escherichia coli
-
 ADP + phosphate + lipid A-core oligosaccharide[side 2]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.5.2.6 Escherichia coli P60752
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.5.2.6 recombinant N-terminally His6-tagged enzyme from isolated Escherichia coli inside-out membrane vesicles by nickel affinity chromatography Escherichia coli

Renatured (Commentary)

EC Number Renatured (Comment) Organism
7.5.2.6 reconstitution of purified MsbA into proteoliposomes, method, overview Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.5.2.6 ATP + H2O + lipid A-core oligosaccharide[side 1]
-
 Escherichia coli ADP + phosphate + lipid A-core oligosaccharide[side 2]
-
 ?
7.5.2.6 ATP + H2O + phosphoethanolamine[side 1] fluorescently NBD (7-nitrobenz-2-oxa-1,3-diazole)-labeled Escherichia coli ADP + phosphate + phosphoethanolamine[side 2]
-
 ?
7.5.2.6 additional information purified MsbA from Escherichia coli displays high ATPase activity, and binds to lipids and lipid-like molecules, including lipid A, with affinity in the low micromolar range. Purified MsbA is reconstituted into proteoliposomes of Escherichia coli lipid and shows ability to translocate 7-nitrobenz-2-oxa-1,3-diazole (NBD)-labeled lipid derivatives. In this system, the protein displays maximal lipid flippase activity of 7.7 nmol of lipid translocated per mg of protein over a 20 min period for an acyl chain-labeled phosphatidylethanolamine derivative. Lipid flippase activity requires ATP hydrolysis, and is dependent on the concentration of ATP and NBD-lipid. MsbA can accommodate lipids with bulky carbohydrate headgroups Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
7.5.2.6 homodimer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.5.2.6 lipid flippase
-
 Escherichia coli
7.5.2.6 MsbA
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.5.2.6 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5.2.6 7.5
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
7.5.2.6 evolution the MsbA protein is an essential ABC (ATP-binding-cassette) superfamily member in Gram-negative bacteria Escherichia coli
7.5.2.6 additional information reconstitution of purified MsbA into proteoliposomes, method, overview Escherichia coli
7.5.2.6 physiological function the homodimeric ATP-dependent lipid translocase or flippase transports lipid A from the inner to the outer leaflet of the cytoplasmic membrane Escherichia coli