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Article

Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane.

The Journal of biological chemistry - 11 Apr 2014

Hayashi Yumi, Tsurumizu Ryoji, Tsukahara Jun, Takeda Kazuki, Narita Shin-Ichiro, Mori Makiko, Miki Kunio, Tokuda Hajime

Abstract excerpt

The Lol system comprising five Lol proteins, LolA through LolE, sorts Escherichia coli lipoproteins to outer membranes. The LolCDE complex, an ATP binding cassette transporter in inner membranes, releases outer membrane-specific lipoproteins in an ATP-dependent manner, causing formation of the LolA-lipoprotein complex in the periplasm. LolA transports lipoproteins through the periplasm to LolB on outer membranes....

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Identifiers

PMID: 24569999
DOI: 10.1074/jbc.M113.539270
PMCID: PMC4036174

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane.PMID 24569999Read ↗

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Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB.Semantic proximity Read ↗

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