This entry represents a domain found in the universal stress protein UspA P28242 [1], which is a small cytoplasmic bacterial protein whose expressionis enhanced when the cell is exposed tostress agents. UspA enhances the rate of cell survival duringprolonged exposure to such conditions, and may provide a general"stress endurance" activity.The crystal structure of Haemophilus influenzae UspA [2] revealsan alpha/beta fold similar to that of the Methanocaldococcus jannaschii (Methanococcus jannaschii)MJ0577 protein, which binds ATP [3], though UspA lacks ATP-bindingactivity.

Proteins containing this domain include the TeaD protein from Halomonas elongata. TeaD regulates the ectoine uptake by the transporter TeaABC. TeaD shows an ATP-dependent oligomerisation [4].

1. Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Mol. Microbiol. 11, 537-44
2. Structure of the universal stress protein of Haemophilus influenzae. Structure 9, 1135-41
3. 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
4. Structure and function of the universal stress protein TeaD and its role in regulating the ectoine transporter TeaABC of Halomonas elongata DSM 2581(T). Biochemistry 49, 2194-204

This entry represents a domain found in the universal stress protein UspA Show more...

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