CellStructureMech

lipopolysaccharide transport system

GO:0062051 · Other · Multiprotein complex · Proposed

A protein-containing complex that functions to transport lipopolysaccharide from its site of synthesis at the cytoplasmic membrane across the periplasm to the outer membrane in an ATP-dependent manner. [GO:0062051]

Synonyms: Lpt machinery; Lpt transenvelope complex

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

ComponentTypePart of / acts onGroundingGenesStoichiometryEssentialRole
LptA periplasmic bridge proteinProteinpart ofReviewed label only (reviewed name; no accession asserted)lptAPeriplasmic bridge constituent that polymerizes between the inner-membrane and outer-membrane Lpt subcomplexes.
  • DOI:10.1128/JB.01126-06 Sperandeo et al. 2007 identified E. coli LptA as a periplasmic protein implicated in LPS transport from the inner to the outer membrane.
  • DOI:10.1126/science.aar1886 Sherman et al. 2018 reconstituted membrane-to-membrane LPS movement through an Lpt protein bridge.
LptB cytoplasmic ATPaseProteinpart ofReviewed label only (reviewed name; no accession asserted)lptBCytoplasmic ATPase constituent that powers LPS extraction by the inner-membrane LptBFGC subcomplex.
  • DOI:10.1128/JB.01126-06 Sperandeo et al. 2007 identified E. coli LptB as an essential protein implicated in LPS transport to the outer membrane.
  • DOI:10.1126/science.1228984 Okuda, Freinkman and Kahne 2012 showed that cytoplasmic ATP hydrolysis powers E. coli LPS transport across the periplasm.
LptC inner-membrane adapterProteinpart ofReviewed label only (reviewed name; no accession asserted)lptCInner-membrane adapter constituent of LptB2FGC that contacts the periplasmic LptA bridge.
LptD outer-membrane beta-barrelProteinpart ofReviewed label only (reviewed name; no accession asserted)lptDOuter-membrane beta-barrel constituent that receives LPS from the periplasmic bridge and participates in final outer-membrane insertion.
  • DOI:10.1073/pnas.0604744103 Wu et al. 2006 identified the E. coli outer-membrane Imp/RlpB, now LptD/LptE, protein complex that assembles LPS in the outer membrane.
  • DOI:10.1073/pnas.0912872107 Chng et al. 2010 characterized LptD as part of the two-protein outer-membrane LptDE complex in E. coli.
LptE outer-membrane lipoproteinProteinpart ofReviewed label only (reviewed name; no accession asserted)lptEOuter-membrane lipoprotein constituent that complexes with LptD in the LPS insertion site.
  • DOI:10.1073/pnas.0604744103 Wu et al. 2006 identified RlpB, now LptE, as the lipoprotein partner of the E. coli outer-membrane LPS assembly complex.
  • DOI:10.1073/pnas.0912872107 Chng et al. 2010 characterized LptE as part of the two-protein outer-membrane LptDE complex in E. coli.
LptF inner-membrane permeaseProteinpart ofReviewed label only (reviewed name; no accession asserted)lptFInner-membrane permease constituent of the LptB2FGC ABC transporter.
  • DOI:10.1073/pnas.0801196105 Ruiz et al. 2008 identified LptF as one of two inner-membrane proteins required for LPS transport to the E. coli outer membrane.
  • DOI:10.1016/j.febslet.2009.05.051 Narita and Tokuda 2009 biochemically characterized the E. coli LptBFGC inner-membrane ABC transporter complex.
LptG inner-membrane permeaseProteinpart ofReviewed label only (reviewed name; no accession asserted)lptGInner-membrane permease constituent of the LptB2FGC ABC transporter.
  • DOI:10.1073/pnas.0801196105 Ruiz et al. 2008 identified LptG as one of two inner-membrane proteins required for LPS transport to the E. coli outer membrane.
  • DOI:10.1016/j.febslet.2009.05.051 Narita and Tokuda 2009 biochemically characterized the E. coli LptBFGC inner-membrane ABC transporter complex.

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Source: data/structures/other/lipopolysaccharide_transport_system.yaml