Format

Send to

Choose Destination
Gene. 1996 Nov 28;181(1-2):103-8.

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.

Author information

1
Department of Biology, University of California at San Diego, La Jolla 92093-0116, USA. jreizer@ucsd.edu

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.

PMID:
8973315
DOI:
10.1016/s0378-1119(96)00481-7
[Indexed for MEDLINE]

Publication types, MeSH terms, Substances, Secondary source ID, Grant support

Publication types

MeSH terms

Substances

Secondary source ID

Grant support

LinkOut - more resources

Full Text Sources

Other Literature Sources

Molecular Biology Databases

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center