InterPro : IPR006015

Name  Universal stress protein A Short Name  Universal_stress_UspA
Type  Family Description  Transcriptional induction of the uspA gene of Escherichia colioccurswhen 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 Uspfamily 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.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

2 Contains

Id Name Short Name Type
IPR006016 UspA UspA Domain
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain

0 Found In

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Freestone P The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis. 1997 J Mol Biol 274 318-24
Zarembinski TI Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. 1998 Proc Natl Acad Sci U S A 95 15189-93

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)