InterPro domain: IPR036523

This entry represents a SurE-like structural domain superfamily with a 3-layer alpha/beta/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.

1. Crystal structure of the stationary phase survival protein SurE with metal ion and AMP. J. Mol. Biol. 371, 123-36
2. Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase. Structure 9, 1095-106
3. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family. Nat. Struct. Biol. 8, 789-94
4. Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity. J. Mol. Biol. 326, 1559-75