Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain

Gene
J ReizerM H Saier

Abstract

Two genes (ptsI and ptsA) that encode homologues of the energy coupling Enzyme I of the phosphoenolpyruvate-dependent sugar-transporting phosphotransferase system (PTS) have previously been identified on the Escherichia coli chromosome. We here report the presence of a third E. coli gene, designated ptsP, that encodes an Enzyme I homologue, here designated Enzyme INtr. Enzyme INtr possesses an N-terminal domain homologous to the N-terminal domains of NifA proteins [(127 amino acids (aa)] joined via two tandem flexible linkers to the C-terminal Enzyme I-like domain (578 aa). Structural features of the putative ptsP operon, including transcriptional regulatory signals, are characterized. We suggest that Enzyme INtr functions in transcriptional regulation of nitrogen-related operons together with previously described PTS proteins encoded within the rpoN operon. It may thereby provide a link between carbon and nitrogen assimilatory pathways.

References

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Citations

Dec 14, 2001·Biochemical and Biophysical Research Communications·P KotrbaH Yukawa
Sep 15, 2001·FEMS Microbiology Letters·M Y GalperinE V Koonin
Jun 1, 1997·Current Opinion in Structural Biology·J Reizer, M H Saier
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Feb 10, 2007·Proceedings of the National Academy of Sciences of the United States of America·Chang-Ro LeeYeong-Jae Seok
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