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Protein Sci. 1992 Jun;1(6):722-6.

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

Author information

1
Department of Biology, University of California, San Diego, La Jolla 92093-0116.

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.

PMID:
1304914
PMCID:
PMC2142240
DOI:
10.1002/pro.5560010604
[Indexed for MEDLINE]
Free PMC Article

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