3.A.1.104.1
Teichoic acid exporter, TagGH.  It is present in a large complex with the teichoic acid precursor synthetic enzymes (Formstone et al. 2008).  The substrate may be the diphospholipid-linked disaccharide portion of the teichoic acid precursor (Schirner et al. 2011).  3-d structural studies have been reported (Ko et al. 2016) showing that TagG and TagH are localized on the cytoplasmic membrane in a patch, and the TMS of TagH is important for normal transport activity (Yamada et al. 2018). The crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site (Yang et al. 2020). The ATPase activity of TagH-N was inhibited by clodronate, a bisphosphonate, in a non-competitive manner, consistent with the proposed wall teichoic acid-binding site for drug targeting (Yang et al. 2020).