Function of the Omp85 Superfamily of Outer Membrane Protein Assembly Factors and Polypeptide Transporters

• Published in: Annual review of microbiology Vol. 76; no. 1; pp. 259 - 279
• Main Authors: Doyle, Matthew Thomas, Bernstein, Harris D
• Format: Journal Article
• Language: English
• Published: United States Annual Reviews 08.09.2022; Annual Reviews, Inc
• Subjects: Antibiotics; Assembly; Bacteria; Gram-negative bacteria; membrane protein insertion; Membrane proteins; Membranes; Organelles; outer membrane; Outer membrane proteins; Polypeptides; protein folding; protein translocation; Protein transport; Proteins; Translocation; β-barrel
• ISSN: 0066-4227; 1545-3251
• DOI: 10.1146/annurev-micro-033021-023719

The Omp85 protein superfamily is found in the outer membrane (OM) of all gram-negative bacteria and eukaryotic organelles of bacterial origin. Members of the family catalyze both the membrane insertion of β-barrel proteins and the translocation of proteins across the OM. Although the mechanism(s) by which these proteins function is unclear, striking new insights have emerged from recent biochemical and structural studies. In this review we discuss the entire Omp85 superfamily but focus on the function of the best-studied member, BamA, which is an essential and highly conserved component of the bacterial barrel assembly machinery (BAM). Because BamA has multiple functions that overlap with those of other Omp85 proteins, it is likely the prototypical member of the Omp85 superfamily. Furthermore, BamA has become a protein of great interest because of the recent discovery of small-molecule inhibitors that potentially represent an important new class of antibiotics.