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An investigation into the Omp85 protein BamK in hypervirulent Klebsiella pneumoniae , and its role in outer membrane biogenesis
Author(s) -
Torres Von Vergel L.,
Heinz Eva,
Stubenrauch Christopher J.,
Wilksch Jonathan J.,
Cao Hanwei,
Yang Ji,
Clements Abigail,
Dunstan Rhys A.,
Alcock Felicity,
Webb Chaille T.,
Dougan Gordon,
Strugnell Richard A.,
Hay Iain D.,
Lithgow Trevor
Publication year - 2018
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13990
Subject(s) - bama , biology , biogenesis , bacterial outer membrane , klebsiella pneumoniae , virulence , membrane protein , function (biology) , genetics , gene , pathogenicity island , mutant , bacteria , microbiology and biotechnology , escherichia coli , membrane
Summary Members of the Omp85 protein superfamily have important roles in Gram‐negative bacteria, with the archetypal protein BamA being ubiquitous given its essential function in the assembly of outer membrane proteins. In some bacterial lineages, additional members of the family exist and, in most of these cases, the function of the protein is unknown. We detected one of these Omp85 proteins in the pathogen Klebsiella pneumoniae B5055, and refer to the protein as BamK. Here, we show that bamK is a conserved element in the core genome of Klebsiella , and its expression rescues a loss‐of‐function ∆ bamA mutant. We developed an E. coli model system to measure and compare the specific activity of BamA and BamK in the assembly reaction for the critical substrate LptD, and find that BamK is as efficient as BamA in assembling the native LptDE complex. Comparative structural analysis revealed that the major distinction between BamK and BamA is in the external facing surface of the protein, and we discuss how such changes may contribute to a mechanism for resistance against infection by bacteriophage.