InterPro: IPR002828 Survival protein SurE-like phosphatase/nucleotidase

This entry represents a SurE-like structural domain with a 3-layer alpha/bete/alpha topology that bears some topological similarity to the N-terminal domain of the glutaminase/asparaginase family. This domain is found in the stationary phase survival protein SurE, a metal ion-dependent phosphatase found in eubacteria, archaea and eukaryotes. In Escherichia coli, SurE also has activity as a nucleotidase and exopolyphosphatase, and may be involved in the stress response [1]. E. coli cells with mutations in the surE gene survive poorly in stationary phase [2]. The structure of SurE homologues have been determined from Thermotoga maritima [3] and the archaea Pyrobaculum aerophilum [4]. The T. maritima SurE homologue has phosphatase activity that is inhibited by vanadate or tungstate, both of which bind adjacent to the divalent metal ion.

This domain is found in acid phosphatases (EC:3.1.3.2), 5'-nucleotidases (EC:3.1.3.5), 3'-nucleotidases (EC:3.1.3.6) and exopolyphosphatases (EC:3.6.1.11).