InterPro : IPR006016

Name  UspA Short Name  UspA
Type  Domain Description  This entry represents a domain found in the universal stress protein UspA [], 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 influenzaeUspA []revealsan alpha/beta fold similar to that of the Methanocaldococcus jannaschii(Methanococcus jannaschii)MJ0577 protein, which binds ATP [], 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 [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

1 Found In

Id Name Short Name Type
IPR006015 Universal stress protein A Universal_stress_UspA Family

1 Parent Features

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

4 Publications

First Author Title Year Journal Volume Pages
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
Nyström T Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. 1994 Mol Microbiol 11 537-44
Sousa MC Structure of the universal stress protein of Haemophilus influenzae. 2001 Structure 9 1135-41
Schweikhard ES Structure and function of the universal stress protein TeaD and its role in regulating the ectoine transporter TeaABC of Halomonas elongata DSM 2581(T). 2010 Biochemistry 49 2194-204



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)