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Structure of the translocator domain of a bacterial autotransporter
Autotransporters are virulence‐related proteins of Gram‐negative bacteria that are secreted via an outer‐membrane‐based C‐terminal extension, the translocator domain. This domain supposedly isExpand
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Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly
After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria,Expand
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Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif
Integral β-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which Omp85Expand
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Biogenesis of the gram-negative bacterial outer membrane.
The cell envelope of gram-negative bacteria consists of two membranes, the inner and the outer membrane, that are separated by the periplasm. The outer membrane consists of phospholipids,Expand
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Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions.
The expression of specific PhoE mutant proteins leads to induction of the expression of the psp operon of Escherichia coli and the export of various plasmid‐encoded precursors is retarded in a pspAExpand
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Interactions between phage-shock proteins in Escherichia coli.
Expression of the pspABCDE operon of Escherichia coli is induced upon infection by filamentous phage and by many other stress conditions, including defects in protein export. Expression of the operonExpand
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Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
Pseudomonas aeruginosa is able to translocate proteins across both membranes of the cell envelope. Many of these proteins are transported via the type II secretion pathway and adopt their tertiaryExpand
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Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica.
The YscC secretin is a major component of the type III protein secretion system of Yersinia enterocolitica and forms an oligomeric structure in the outer membrane. In a mutant lacking the outerExpand
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Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein.
Bacterial outer membrane proteins are supposed to span the membrane repeatedly, mostly in the form of amphipathic beta-sheets. The last ten C-terminal amino acid residues of PhoE protein are supposedExpand
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The C Terminus of SecA Is Involved in Both Lipid Binding and SecB Binding (*)
Using C-terminal deletion mutations in secA, we localized the previously proposed (Breukink, E., Keller, R. C. A., and de Kruijff, B.(1993), FEBS Lett. 331, 19-24) second lipid binding site on SecA.Expand
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