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Literature summary extracted from

  • Schultz, K.M.; Lundquist, T.J.; Klug, C.S.
    Lipopolysaccharide binding to the periplasmic protein LptA (2017), Protein Sci., 26, 1517-1523 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.43 gene lptA, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.8.43 I36R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 I36R1/Q148A/K149A site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 I86R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 I86R1/Q148A/K149A site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 L145R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 L45R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 M98R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 N185R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 N185R1/Q148A/K149A site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 Q148A/K149A site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 S110R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 T32R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 V132R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli
2.7.8.43 V165R1 site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.8.43 periplasm possibly one or more LptA proteins bridges the periplasm to form a large, connected protein complex Escherichia coli
-
-
7.5.2.6 inner membrane an integral transmembrane protein Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.5.2.6 Mg2+ required Escherichia coli

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
2.7.8.43 Escherichia coli P0ADV1
-
-
7.5.2.6 Escherichia coli P60752
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.8.43 recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by cobalt affinity chromatography, dialysis, and ultrafiltration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.43 additional information quantitative analysis of binding of LPS by LptA, 1:1 ratio for the LPS:LptA complex, and structure analysis of the LPS binding pocket. The entire LptA protein is affected by LPS binding, the N-terminus unfolds in the presence of LPS Escherichia coli ?
-
 ?
7.5.2.6 ATP + H2O + lipid A-core oligosaccharide[side 1]
-
 Escherichia coli ADP + phosphate + lipid A-core oligosaccharide[side 2]
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.8.43 More according to light scattering data, LptA oligomerizes in a concentration-dependent manner. LptA is an average of a trimer in solution, and a considerably higher order oligomerization state (25mers) is predicted at a protein concentration of 0.1 mM Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.8.43 LptA
-
 Escherichia coli
7.5.2.6 EcMsbA
-
 Escherichia coli
7.5.2.6 lipid A export ATP-binding/permease protein MsbA UniProt Escherichia coli
7.5.2.6 MsbA
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.8.43 37
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.5.2.6 ATP
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.8.43 evolution LptA is a member of the lipopolysaccharide transport protein (Lpt) family Escherichia coli
2.7.8.43 malfunction a mutant LptA protein unable to form oligomers has an altered affinity for LPS Escherichia coli
2.7.8.43 physiological function LptA functions to transport lipopolysaccharide (LPS) through the periplasm to the outer leaflet of the outer membrane after ABC transporter MsbA flips LPS across the inner membrane. It is hypothesized that LPS binds to LptA to cross the periplasm and that the acyl chains of LPS bind to the central pocket of LptA Escherichia coli
7.5.2.6 additional information structure comparisons and molecular basis of active lipid transport, overview Escherichia coli
7.5.2.6 physiological function the movement of core-lipopolysaccharide across the inner membrane of Gram-negative bacteria is catalysed by an essential ATP-binding cassette transporter, MsbA. The ABC transporter MsbA flips the lipid to the outer leaflet of the inner membrane and the O-antigen is attached by WaaL to create LPS. LPS and the periplasmic protein, LptA (EC 2.7.8.43), are two essential components of Gram-negative bacteria. LPS (endotoxin) is asymmetrically distributed in the outer leaflet of the outer membrane of Gram-negative bacteria such as Escherichia coli and plays a role in the organism's natural defense in adverse environmental conditions. LptA is a member of the lipopolysaccharide transport protein (Lpt) family, which also includes LptC, LptDE, and LptBFG2, that functions to transport LPS through the periplasm to the outer leaflet of the outer membrane after MsbA flips LPS across the inner membrane Escherichia coli