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Microbiology and Molecular Biology Reviews, December 2005, p. 608-634, Vol. 69, No. 4
1092-2172/05/$08.00+0 doi:10.1128/MMBR.69.4.608-634.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Comparative Genomic Analyses of the Bacterial Phosphotransferase System
Ravi D. Barabote and
Milton H. Saier Jr.*
Division of Biological Sciences, University of California at San Diego, La Jolla, California 92093-0116
We
report analyses of 202 fully sequenced genomes for homologues of known
protein constituents of the bacterial phosphoenolpyruvate-dependent
phosphotransferase system (PTS). These included 174 bacterial, 19
archaeal, and 9 eukaryotic genomes. Homologues of PTS proteins were not
identified in archaea or eukaryotes, showing that the horizontal
transfer of genes encoding PTS proteins has not occurred between the
three domains of life. Of the 174 bacterial genomes (136 bacterial
species) analyzed, 30 diverse species have no PTS homologues, and 29
species have cytoplasmic PTS phosphoryl transfer protein homologues but
lack recognizable PTS permeases. These soluble homologues presumably
function in regulation. The remaining 77 species possess all PTS
proteins required for the transport and phosphorylation of at least one
sugar via the PTS. Up to 3.2% of the genes in a bacterium encode PTS
proteins. These homologues were analyzed for family association, range
of protein types, domain organization, and organismal distribution.
Different strains of a single bacterial species often possess
strikingly different complements of PTS proteins. Types of PTS protein
domain fusions were analyzed, showing that certain types of domain
fusions are common, while others are rare or prohibited. Select PTS
proteins were analyzed from different phylogenetic standpoints, showing
that PTS protein phylogeny often differs from organismal phylogeny. The
results document the frequent gain and loss of PTS protein-encoding
genes and suggest that the lateral transfer of these genes within the
bacterial domain has played an important role in bacterial evolution.
Our studies provide insight into the development of complex
multicomponent enzyme systems and lead to predictions regarding the
types of protein-protein interactions that promote efficient
PTS-mediated phosphoryl transfer.
* Corresponding
author. Mailing address: Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116. Phone: (858)
534-4084. Fax: (858) 534-7108. E-mail:
msaier{at}ucsd.edu.
Microbiology and Molecular Biology Reviews, December 2005, p. 608-634, Vol. 69, No. 4
1092-2172/05/$08.00+0 doi:10.1128/MMBR.69.4.608-634.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
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