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(Received for publication, July 10, 1996, and in revised form, August 20, 1996)
From the Department of Microbiology, University of Guelph, Guelph,
Ontario N1G 2W1, Canada
The plasmid-encoded gene cluster for O:54
O-polysaccharide synthesis in Salmonella enterica serovar
Borreze (rfbO:54) contains three genes that
direct synthesis of a ManNAc homopolymer with alternating
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28581-28592
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
1,3 and
1,4 linkages. In Escherichia coli K-12,
RfbAO:54 adds the first ManNAc residue to the Rfe
(UDP-GlcpNAc::undecaprenylphosphate
GlcpNAc-1-phosphate transferase)- modified
lipopolysaccharide core. Hydrophobic cluster analysis of
RfbAO:54 indicates this protein belongs to the ExoU family
of nonprocessive -glycosyltransferases. Two putative catalytic
residues and a potential substrate-binding motif were
identified in RfbAO:54. Topological analysis of
RfbBO:54 predicts four transmembrane domains and a large
central cytoplasmic domain. The latter shares homology with a similar
domain in the processive -glycosyltransferases Cps3S of
Streptococcus pneumoniae and HasA of Streptococcus
pyogenes. Hydrophobic cluster analysis of RfbBO:54
and Cps3S indicates both possess the structural features characteristic
of the HasA family of processive -glycosyltransferases. Four
potential catalytic residues and a putative substrate-binding motif
were identified in RfbBO:54. In 
rfb E. coli
K-12, RfbAO:54 and RfbBO:54 direct synthesis of
smooth O:54 lipopolysaccharide, indicating that this O-polysaccharide
involves a novel pathway for O-antigen transport. Based on sequence and
structural conservation, 15 new ExoU-related and 17 new HasA-related
transferases were identified.
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