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GTPase HflX
GTPase HflX is a GTP-binding protein with a GTP hydrolysis activity that is stimulated by binding to the 50S ribosome subunit; it may play a role during protein synthesis or ribosome biogenesis
This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like).
ribosome rescue GTPase HflX
Involved in modulation of proteins HflK and HflC; part of the hflA locus (high frequency of lysogenization) which governs the lysis-lysogeny decision of bacteriophage lambda by controlling stability of the phage cII protein
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