A specialised system involved in a diverse array of functions, including the biogenesis of fimbriae, protein secretion and DNA uptake, has recently been found to be widespread in the eubacteria. These systems have in common several sets of related genes, including those encoding proteins containing leader sequences homologous to that of the type-4 fimbrial subunit (prepilin), a prepilin-type leader peptidase, a cytoplasmic nucleotide-binding protein, and other proteins located in the inner and outer membranes [Hobbs, M. and Mattick, J.S., Mol Microbiol. 10 (1993) 233-243]. Here, we show that Escherichia coli contains at least nine homologs of this system, and present complete sequence data for five of the genes involved (ppdD. hopB, hopC, hopD and pshM), as well as for an adjacent gene (nadC), which encodes quinolic acid phosphoribosyltransferase. Insertional mutagenesis of hopB and hopD failed to reveal any obvious effects on cell viability, morphogenesis of M13 phage, conjugative transfer of the F plasmid, or protein secretion.