InterPro domain: IPR035651

This domain describes the C-terminal portion of BipA (or TypA) having homology to the domain V of the elongation factors EF-G [ 1 ]. A member of the ribosome binding GTPase superfamily, BipA is widely distributed in bacteria and chloroplasts [ 2 ]. It has been implicated in regulating a variety of cellular processes, including bacterial virulence and various stress responses [ 3 , 4 , 5 , 6 ].BipA is phosphorylated on a tyrosine residue under some cellular conditions [ 7 ].

BipA contains domains that are homologous EF-G domain I, II, III, V. This entry represent the domain that is homologous to domain V.

1. Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function. RNA Biol 13, 1258-1273
2. Phylogenetic distribution of translational GTPases in bacteria. BMC Genomics 8, 15
3. Co-ordination of pathogenicity island expression by the BipA GTPase in enteropathogenic Escherichia coli (EPEC). Mol. Microbiol. 48, 507-21
4. TypA is involved in virulence, antimicrobial resistance and biofilm formation in Pseudomonas aeruginosa. BMC Microbiol. 13, 77
5. The typA gene is required for stress adaptation as well as for symbiosis of Sinorhizobium meliloti 1021 with certain Medicago truncatula lines. Mol. Plant Microbe Interact. 17, 235-44
6. BipA is required for growth of Escherichia coi K12 at low temperature. Mol. Genet. Genomics 266, 313-7
7. BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells. Mol. Microbiol. 28, 265-79