InterPro domain: IPR042116

The translational GTPase BipA (also known as TypA or YihK) regulates the expression of virulence and pathogenicity factors in several eubacteria. BipA-dependent expression of virulence factors occurs under starvation conditions, such as encountered during infection of a host. BipA is composed of five domains. Domain I consists of a central six-stranded beta-sheet surrounded by five alpha-helices, which is characteristic for the G domain found in translational GTPases. Domain II has the distinctive OB-fold of oligonucleotide/oligosaccharide binding domains. Domains III and V both have the same double-split beta-alpha-beta fold. The C-terminal domain of BipA spatially occupies a position between domains III and V and consists of a unique mixed alpha + beta fold composed of eight beta-sheets and two alpha-helices [ 1 ].

This superfamily represents the C-terminal domain found in GTP-binding protein TypA/BipA.

1. Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. J. Biol. Chem. 290, 20856-64