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Literature summary for 3.1.7.2 extracted from

  • Gratani, F.; Horvatek, P.; Geiger, T.; Borisova, M.; Mayer, C.; Grin, I.; Wagner, S.; Steinchen, W.; Bange, G.; Velic, A.; Macek, B.; Wolz, C.
    Regulation of the opposing (p)ppGpp synthetase and hydrolase activities in a bifunctional RelA/SpoT homologue from Staphylococcus aureus (2018), PLoS Genet., 14, e1007514 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
ribosome the C-terminal domain interacts with the ribosome, which is largely dependent on the TGS motif Staphylococcus aureus 5840
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Organism

Organism UniProt Comment Textmining
Staphylococcus aureus W8U368 bifunctional (p)ppGpp synthase/hydrolase SpoT, catalyzes reactions of EC 2.7.6.5 and EC 3.1.7.2
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General Information

General Information Comment Organism
physiological function in vivo, under relaxed conditions, as well as in vitro, the C-terminal regulatory domain CTD inhibits synthetase activity but is not required for hydrolase activity. Under stringent conditions, the CTD is essential for (p)ppGpp synthesis. A mutant lacking the CTD exhibits net hydrolase activity when expressed in Staphylococcus aureus but net (p)ppGpp synthetase activity when expressed in Escherichia coli. The conserved TGS and DC motifs within the CTD are required for correct stringent response, whereas the conserved ACT motif is dispensable. The enzyme primarily exists in a synthetase-off/hydrolase-on state Staphylococcus aureus