Abstract
Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) constitute a large family of proteases secreted by Escherichia coli and Shigella. SPATEs exhibit two distinct proteolytic activities. First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. Second, the secreted N-terminal domains of SPATEs are themselves proteases; each contains a canonical serine-protease catalytic site. Some of these secreted proteases are toxins, eliciting various effects on mammalian cells. Here, we discuss the biogenesis of SPATEs and their function as toxins.
Highlights
(EHEC plasmid-encoded autotransporter) from enterohaemorrhagic E. coli (EHEC) [14,15,16], Pet from enteroaggregative E. coli (EAEC) [17], Pic from EAEC, uropathogenic E. coli (UPEC) and Shigella [18,19], EspC
Proteins belonging to the SPATE family display the typical characteristics of autotransporters: they are composed of a signal sequence, a passenger domain secreted in the extracellular medium, and a
SPATEs were initially identified as proteins secreted by bacterial species that are pathogenic to humans or animals
Summary
SPATE (Serine Protease Autotransporters of Enterobactericeae) is a family of extracellular proteases produced by the Enterobacteriaceae. 30 amino acid residues, located upstream from the -barrel-forming region in the primary sequence, form an -helix in the pore of the -barrels and connect the N-terminus of the -barrel with the extracellular passenger domain (Figure 1). This region, called the “linker domain” is necessary for the folding and stability of the -barrel [10,12,13]. One of them is the SPATE subfamily, initially identified by Henderson et al [2]
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