InterPro domain: IPR006016

This entry represents a domain found in the universal stress protein UspA [ 1 ], which is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged 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-binding activity.

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