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Literature summary for 2.7.8.43 extracted from

  • Sherman, D.J.; Lazarus, M.B.; Murphy, L.; Liu, C.; Walker, S.; Ruiz, N.; Kahne, D.
    Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport (2014), Proc. Natl. Acad. Sci. USA, 111, 4982-4987 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
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 Neisseria meningitidis serogroup B
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-

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis serogroup B Q7DDQ9
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Neisseria meningitidis serogroup B MC58 Q7DDQ9
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-

Synonyms

Synonyms Comment Organism
LptA
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 Neisseria meningitidis serogroup B
LptH
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 Neisseria meningitidis serogroup B

General Information

General Information Comment Organism
malfunction the phenotypes of Neisseria meningitidis strains lacking LptB, LptC, LptH (homologue of Escherichia coli LptA), LptF, and LptG are identical to those lacking LptD or MsbA, i.e. the knockout mutants are viable but leaky and produce only very little LPS, which is not present at the cell surface Neisseria meningitidis serogroup B
physiological function the enzyme is involved in lipopolysaccharide (LPS) transport. LptA binds lipid A, it might act as a chaperone, assisting the amphipathic LPS molecules to pass through the aqueous periplasm. LptB, LptC, LptF, LptG, and LptH(LptA) are essential components of the LPS transport system in the important model organism for outer membrane biogenesis, Neisseria meningitidis, as they are in Escherichia coli. LptA binds to LptC but not to LptE Neisseria meningitidis serogroup B