The autoinducer-2 exporter superfamily

Abstract

The TqsA (YdgG) protein of Escherichia coli has been shown to export the autoinducer-2 (AI-2) molecule, a furanosyl borate diester that bears little resemblance to previously characterized biological molecules. TqsA belongs to a large superfamily, the AI-2 exporter (AI-2E) superfamily, of putative transporters with no other functionally characterized members. These proteins derive exclusively from bacteria. Many different bacterial kingdoms contain them, although several kingdoms do not. These proteins exhibit a uniform topology with 8 putative transmembrane segments (TMSs) which we show probably arose from a 4-TMS precursor in a process that involved at least one and possibly two intragenic duplication event(s). The first halves of these proteins are more diverse in sequence than the second halves, suggesting that the first halves may serve substrate-specific functions while the second halves serve family-specific functions. Conserved residues and motifs in these proteins are identified. Some homologues include extra catalytic domains including those involved in purine nucleotide biosynthesis, ATP and GTP binding, and molecular signaling. The results presented provide guides for future functional studies on members of this superfamily of bacterial transporters.