| Primary Identifier | IPR004565 | Type | Family |
| Short Name | OM_lipoprot_LolB |
| description | This protein, LolB, is known so far only in the gamma subdivision of the Proteobacteria. It is a processed, lipid-modified outer membrane protein. In Escherichia coli, lipoproteins are anchored to theperiplasmic side of either the inner or outer membrane through N-terminal lipids, depending on the lipoprotein-sorting signal present atposition 2 []. Five Lol proteins are involved in the sorting and outer membrane localization of lipoproteins. LolCDE, an ATPbinding 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 LolA. The LolA-lipoprotein complex crosses the periplasm and theninteracts with outer membrane receptor LolB, which is essential for the anchoring of lipoproteins to the outer membrane. |
