v5.1.0.3
Glycine data from LIS
Type | Family |
Description | Transcriptional induction of the uspA gene of Escherichia coli occurs 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 β-sheet with 2 helices on each side of the sheet []. 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 [ ]. |
Short Name | Universal_stress_UspA |