Membrane spanning protein in tola-tolq-tolr complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity . Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction .The Tol-Pal system is also required for polar localization of chemoreceptors clusters (Probable). There are about 900 TolR molecules per cell . Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglyca [...]

Peptidoglycan-associated outer membrane lipoprotein pal; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity The Tol-Pal system is also required for polar localization of chemoreceptors clusters

Periplasmic tola-binding protein; Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division. Promotes physical and functional coordination of the PBP1B-LpoB and Tol machines, and regulates PBP1B activity in response to Tol energy state

Membrane anchored protein in tola-tolq-tolr complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity Is also involved in the uptake of group A colicins (colicins A, E1, E2, E3, and K) and in the uptake of filamentous phage DNA . The Tol-Pal system is also required for polar localization of chemoreceptors clusters

Outer membrane porin 1a (ia;b;f); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity

Acyl-coa thioester hydrolase; Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond

An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . The only protein known to be covalently linked to the peptidoglycan network (PGN) . Also non-covalently binds the PGN . The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...]

With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape . Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes . A very abundant protein, there can be up to 210,000 OmpA molecules per cell . Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at [...]

Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...]