This map is an update of the edition 9 map by Berlyn et al.(MKB Berlyn, KB Low, and KE
Rudd, p. 1715–1902, in FC Neidhardt et al., ed., Escherichia coli and Salmonella: cellular …

About 30% of all bacterial proteins execute their function outside of the cytosol and have to
be transported into or across the cytoplasmic membrane. Bacteria use multiple protein …

When secY is overexpressed over secE or secE is underexpressed, a fraction of SecY
protein is rapidly degraded in vivo. This proteolysis was unaffected in previously described …

Bacterial periplasmic nickel-containing hydrogenases are composed of a small subunit
containing a twin-arginine signal sequence and a large subunit devoid of an export signal …

The trimethylamine N‐oxide (TMAO) reductase of Escherichia coli is a soluble periplasmic
molybdoenzyme. The precursor of this enzyme possesses a cleavable N‐terminal signal …

The product of the Escherichia coli secM gene (secretion monitor, formerly gene X),
upstream of secA, is involved in secretion-responsive control of SecA translation. In wild …

Escherichia coli FtsH (HflB), a membrane‐bound ATPase is required for proteolytic
degradation of uncomplexed forms of the protein translocase SecY subunit. We have now …

The bacterial twin arginine translocation (Tat) pathway is capable of exporting cofactor-
containing enzymes into the periplasm. To assess the capacity of the Tat pathway to export …

Most membrane proteins are co-translationally inserted into the lipid bilayer via the
universally conserved SecY complex and they access the lipid phase presumably via a …

Several antibacterial compounds have recently been discovered that potentially inhibit the
activity of BamA, an essential subunit of a heterooligomer (the b arrel a ssembly m achinery …