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LPS is synthesized at the inner membrane and then transported to the outer leaflet of the outer membrane. Although the overall LPS structure is conserved, LPS molecules can differ in composition at the species and strain level. Some bacteria also regulate when to modify phosphates on LPS at the inner membrane in order to become resistant to cationic antimicrobial peptides. The multi\u2010protein Lpt trans\u2010envelope machine, which transports LPS from the inner to the outer membrane, must therefore handle a variety of substrates. The most poorly understood step in LPS transport is how the ATP\u2010binding cassette LptB<jats:sub>2<\/jats:sub>FG transporter extracts LPS from the inner membrane. Here, we define residue K34 in LptG as a site within the structural cavity of the <jats:italic>Escherichia coli<\/jats:italic> LptB<jats:sub>2<\/jats:sub>FG transporter that interacts electrostatically with phosphates on unmodified LPS. Alterations to this residue cause transport defects that are suppressed by the activation of the BasSR two\u2010component signaling system, which results in modifications to the LPS phosphates. We also show this residue is part of a larger site in LptG that differentially contributes to the transport of unmodified and modified LPS.<\/jats:p>","DOI":"10.1111\/mmi.14059","type":"journal-article","created":{"date-parts":[[2018,7,11]],"date-time":"2018-07-11T16:30:11Z","timestamp":1531326611000},"page":"541-554","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["A cluster of residues in the lipopolysaccharide exporter that selects substrate variants for transport to the outer membrane"],"prefix":"10.1111","volume":"109","author":[{"given":"Blake R.","family":"Bertani","sequence":"first","affiliation":[{"name":"Department of Microbiology The Ohio State University Columbus OH 43210 USA."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rebecca J.","family":"Taylor","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology Harvard University Cambridge MA 02138 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