It is found that the leader peptide and the N-terminal 17 amino acid residues of mature XcpT could be functionally replaced by the corresponding part of PilA, which shows that this domain of the protein does not contain information for targeting to the Xcp system.
XcpS domains were identified that are important for species-specific functioning and thus represent putative interaction domains and the cytoplasmic loop of XcpS was found to be involved in the stabilization by XcpR and XcpY.
Key determinants of secretion specificity and endopilus stability are identified, revealing how minor sequence variations in conserved nanomachines drive functional adaptation to diverse environments.
The extent to which chaperones are universally required for effector secretion is evaluated, through analysis of the conservation of chaperone sequence and structure, to discuss how these proteins interact with and support the secretion of diverse substrates.
It is proposed that the binding of a cognate DNA substrate triggers the T4CP to suppress pilus production by blocking elongation, or stimulating retraction or release, which transitions the T4SS from its default pilus-generating (mate-seeking) mode to the activated DNA-translocation (mating) machine.
TpeX is identified as a bactericidal, colicin-like pore-forming T6SS effector whose membrane activity is controlled by a cognate immunity protein, thereby expanding the repertoire of membrane-targeting weapons used by P. aeruginosa in interbacterial competition.
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