Member database | Pfam |
Pfam type | family |
Short name | LolB |
Clan | LolA_LolB |
Author | TIGRFAMs; Griffiths-Jones SR;0000-0001-6043-807X |
Sequence Ontology | 0100021 |
Description Imported from IPR004565
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 the periplasmic side of either the inner or outer membrane through N-terminal lipids, depending on the lipoprotein-sorting signal present at position 2
[1]. 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 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.
References Imported from IPR004565
1.Elucidation of the function of lipoprotein-sorting signals that determine membrane localization. Masuda K, Matsuyama S, Tokuda H. Proc. Natl. Acad. Sci. U.S.A. 99, 7390-5, (2002). View articlePMID: 12032293
Integrated to
Representative structure
3wjt: Crystal structure of the L68D variant of mLolB