EC Number   |
General Information |
Reference |
|---|
    3.1.7.2 | malfunction |
Mesh1 deletion impairs starvation resistance in Drosophila, overview |
716313 |
| 3.1.7.2 | more |
crucial residues for the ppGpp hydrolysis activity of Mesh1 are Arg24, Glu65, Asp66 and Asn126 |
716313 |
| 3.1.7.2 | physiological function |
anti-sigma factor Rsd directly interacts with SpoT and stimulates its (p)ppGpp hydrolase activity. Dephosphorylated histidine-containing phosphocarrier protein HPr of the phosphoenolpyruvate-dependent sugar phosphotransferase system can antagonize the stimulatory effect of Rsd on SpoT (p)ppGpp hydrolase activity |
752064 |
| 3.1.7.2 | 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 |
751910 |
| 3.1.7.2 | physiological function |
SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. The phosphorylated version of EIIANtr interacts directly with the ACT and inhibits the hydrolase activity of SpoT |
-, 751760 |
| 3.1.7.2 | physiological function |
the level of ppGpp controls the length of diauxic lag via control of the level of acetyl phosphate |
750643 |
