Outer membrane lipoprotein carrier protein LolA, Proteobacteria (IPR018323)

Short name: OM_lipoprot_carrier_LolA_Pbac

Overlapping homologous superfamilies

Family relationships


In Escherichia coli, lipoproteins are anchored to the periplasmic side of either the inner or outer membrane through N-terminal lipids, depending on the lipoprotein-sorting signal present at position 2 [PMID: 12032293]. Five Lol proteins are involved in the sorting and outer membrane localization of lipoproteins. LolCDE, an ATP binding cassette (ABC) transporter, in the inner membrane releases outer membrane-directed lipoproteins from the inner membrane in an ATP-dependent manner, leading to the formation of a water-soluble complex between the lipoprotein and the molecular chaperone, LolA. The LolA-lipoprotein complex crosses the periplasm and then interacts with outer membrane receptor LolB, which is essential for the anchoring of lipoproteins to the outer membrane [PMID: 19716823, PMID: 20620146].

E. coli lipoproteins are anchored to the inner or outer membrane depending on the residue at position 2. Aspartate at this position makes lipoproteins specific to the inner membrane, whereas other residues cause the release of lipoproteins from the inner membrane [PMID: 20419407].

GO terms

Biological Process

GO:0042953 lipoprotein transport

Molecular Function

GO:0042954 lipoprotein transporter activity

Cellular Component

GO:0042597 periplasmic space

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.