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. 1992 Jun;1(6):722–726. doi: 10.1002/pro.5560010604

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

J Reizer 1, A Reizer 1, M H Saier Jr 1, G R Jacobson 1
PMCID: PMC2142240  PMID: 1304914

Abstract

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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Selected References

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