<p>Proteins in this group are stand-alone YeaR proteins, the predication is based on domain association, and is known to be involved in tellurite resistance.</p> <p>Tellurite resistance protein TehB is encoded by the tellurite-reducing operon <i>tehAB</i> [<cite idref="PUB00027707"/>]. TehB exists in a two-domain form (<db_xref db="INTERPRO" dbkey="IPR014431"/>) with a C-terminal SAM-dependent methyltransferase domain and an N-terminal domain of unknown function; and in the form of two stand-alone proteins: YeaR protein (this group) and single-domain TehB methyltransferase (<db_xref db="INTERPRO" dbkey="IPR014641"/>).</p> <p>When upregulated or present in high copy number, TehB of <taxon tax_id="1313">Streptococcus pneumoniae</taxon> is responsible for potassium tellurite resistance, this is achieved by increasing the reduction rate of tellurite to metallic tellurium within the bacterium. TehB is a cytoplasmic protein that possesses three conserved motifs (I, II, and III) found in S-adenosyl-L-methionine (SAM)-dependent non-nucleic acid methyltransferases [<cite idref="PUB00014885"/>]. Conformational changes in TehB are observed upon binding of both tellurite and SAM, suggesting that TehB utilises a methyltransferase activity in the detoxification of tellurite [<cite idref="PUB00027741"/>].</p> <p>The role of YeaR protein and of the corresponding domain in two-domain TehB in tellurite resistance is not known.</p> Tellurite resistance predicted, YeaR