InterPro domain: IPR006015

Transcriptional induction of the uspA gene of Escherichia coli occurswhen conditions cause growth arrest; cells deficient in UspA survivepoorly in stationary phase [ 1 ]. The product of uspA has been shown to bea cytoplasmic serine and threonine phosphoprotein. Members of the Uspfamily are predicted to be related to the MADS-box proteins and bind to DNA[ 2 ]. Some members of the family contain 2 copies of the domain.

The structure of a UspA homologue from Methanocaldococcus jannaschii (Methanococcus jannaschii) from has been determined to 1.8 angstroms resolution by using its selenomethionyl derivativeand multiwavelength anomalous diffraction. The protein homodimerises in the crystal; each monomer adopts an open-twisted 5-stranded parallel beta-sheet with 2 helices on each side of the sheet [ 2 ]. Although the structureco-crystallised with ATP, the function of the protein is unknown.

This entry includes five E. coli Usp paralogues: uspA, uspC, uspD, uspF and uspG [ 3 ].

1. The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis. J. Mol. Biol. 274, 318-24
2. Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. Proc. Natl. Acad. Sci. U.S.A. 95, 15189-93
3. The bacterial universal stress protein: function and regulation. Curr. Opin. Microbiol. 6, 140-5