Protein Science, Vol 1, Issue 6 722-726, Copyright © 1992 by Cold Spring Harbor Laboratory Press

ARTICLE

A proposed link between nitrogen and carbon metabolism involving protein phosphorylation in bacteria

J. REIZER, A. REIZER, M. H. SAIER-JR. and G. R. JACOBSON
Department of Biology, University of California at San Diego, La Jolla, California 92093-0116

We demonstrate that certain phosphoryl transfer proteins of the bacterial phosphotransferase system (PTS), the fructose- and mannitol-specific IIA proteins or domains, are homologous to a class of proteins, one of which is known to affect transcription of some of the nitrogen-regulatory {sigma}(54)-dependent operons in Klebsiella pneumoniae. The phosphorylatable histidyl residue in the homologous PTS proteins and the consensus sequence in the vicinity of the active-site histidine are fully conserved in all members that comprise this family of proteins. A phylogenetic tree of the eight protein members of this family was constructed, and a ``signature'' sequence that can serve for the identification of new protein members of this family is proposed. These observations suggest that PTS-catalyzed protein phosphorylation may provide a regulatory link between carbon and nitrogen assimilation in bacteria.
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