The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
phosphoethanolamine transferase, petn transferase, pea transferase, lipid a phosphoethanolamine transferase, cj0256, esa_rs09200, lipooligosaccharide phosphoethanolamine transferase a, hp0022, lpt-o, phosphoethanolamine transferase a, more
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
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
A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2+ hypersensitivity of an eptB deletion mutant.
Modification of lipooligosaccharide with phosphoethanolamine by LptA in Neisseria meningitidis enhances meningococcal adhesion to human endothelial and epithelial cells.
Phosphoethanolamine Decoration of Neisseria gonorrhoeae Lipid A Plays a Dual Immunostimulatory and Protective Role during Experimental Genital Tract Infection.
Effects of neonatal undernutrition of rats on the synthesis of phosphatidylcholine and phosphatidylethanolamine by microsomes from gray matter and white matter.
Phosphoethanolamine Decoration of Neisseria gonorrhoeae Lipid A Plays a Dual Immunostimulatory and Protective Role during Experimental Genital Tract Infection.
LptA is the only component of the Lpt system that lacks a transmembrane component, as it spans the periplasmic space between the inner membrane and outer membrane complexes. LptA is bound to other Lpt components rather than floating freely in the periplasm
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
the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit, functional significance of LptA oligomerization and LptC. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the outer membrane by periplasmic LptA. The LptB2FG tetramer extracts LPS from the outer leaflet of the inner membrane and provides the energy to drive LPS transport through an ATPase-dependent mechanism. LptA provides a continuous LPS binding surface that conveys it to the outer membrane. Mechanism of the LPS (lipopolysaccharide) transport (Lpt) system, specific LPS interactions with LptA and LptC, LptC is the intermediate between the inner membrane complex and LptA, overview
the enzyme LptA arranges in an end-to-end fibrous tetramer, which forms a continuous hydrophobic groove between the LptA monomers, crystal structure analysis. Mass spectral analysis confirmes that LptA forms 2-5-member oligomers in a concentration-dependent manner when purified in vitro and that the resultant complexes are stabilized by LPS. Analysis of subunit interactions
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by cobalt affinity chromatography, dialysis, and ultrafiltration