Bacterial outer membrane proteins are recognized by BamD at specific signals located in multiple β-strands at the C-terminus of these proteins, and this recognition is important for efficient outer membrane protein assembly and maintaining the integrity of outer membrane.

Phylogenomics provides support for the Gram-positive type of bacterial cell envelope being a derived character that arose independently multiple times through loss of an ancestral outer membrane.

Auxiliary proteins play functional roles in modulating the assembly and activity of a non-canonical ABC transporter that is important for the maintenance of outer membrane lipid asymmetry.

Uniform diameter and curvature of the outer membrane extensions and vesicles of Shewanella oneidensis are maintained by a bacterial Bin/Amphiphysin/Rvs (BAR) domain-like protein BdpA.

Electron cryo-tomography reveals that bacteria can form structurally-diverse outer membrane extensions with various protein complexes associated with them.

The envelope stress factor DolP associates with the outer membrane protein assembly machinery and supports proper folding and functioning of BamA contributing to preserve envelope integrity.

The protein translocation apparatus of the inner- (Sec) and outer-membrane (BAM) interact to form a trans-periplasmic super-complex capable of long-range, PMF-dependent conformational changes to facilitate efficient outer-membrane protein maturation.

There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

The damage of the bacterial cell envelope is found to be only a secondary effect of the antimicrobial activity of lactoferricin derivatives.

Structure of MlaFB reveals how a small binding protein and the C-terminal tail on an ATPase subunit work together to regulate the assembly and function of an ABC transporter.