<p>This group represents a chaperone HchA. Hsp31 is the product of the sigmaS- and sigmaD- dependent hchA gene in <taxon tax_id="562">Escherichia coli</taxon>. It is a molecular chaperone whose activity is inhibited by ATP at high temperatures [<cite idref="PUB00044118"/>]. This heat-inducible chaperone is implicated in the management of protein misfolding at high temperatures and plays an important role in the acid resistance of starved E. coli, but it has little influence on oxidative-stress survival [<cite idref="PUB00044119"/>]. Hsp31 is a homodimeric member of the ThiI/DJ-1/PfpI superfamily that has the activities of both a molecular chaperone and an aminopeptidase. Little is known about the regulation of the hchA gene. It is transcribed from dual promoters recognised by the sigmaD (sigma70) and sigmaS (sigma38) subunits of RNA polymerase (E) [<cite idref="PUB00044120"/>].</p> Chaperone, HchA