| Type: | Family | Name: | Universal stress protein A |
| Description: | Transcriptional induction of the uspA gene of Escherichia colioccurs when conditions cause growth arrest; cells deficient in UspA survivepoorly in stationary phase []. The product of uspA has been shown to bea cytoplasmic serine and threonine phosphoprotein. Members of the Usp family are predicted to be related to the MADS-box proteins and bind to DNA[]. 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 []. Although the structureco-crystallised with ATP, the function of the protein is unknown. | Short Name: | Universal_stress_UspA |
