Phosphotransferase system (PTS) - Polaromonas naphthalenivorans
The phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) is a major mechanism used by bacteria for uptake of carbohydrates, particularly hexoses, hexitols, and disaccharides, where the source of energy is from PEP. The PTS consists of two general components, enzyme I (EI) and histidine phosphocarrier protein (HPr), and of membrane-bound sugar specific permeases (enzymes II). Each enzyme II (EII) complex consists of one or two hydrophobic integral membrane domains (domains C and D) and two hydrophilic domains (domains A and B). EII complexes may exist as distinct proteins or as a single multidomain protein. The PTS catalyzes the uptake of carbohydrates and their conversion into their respective phosphoesters during transport. There are four successive phosphoryl transfers in the PTS. Initial autophosphorylation of EI, using PEP as a substrate, is followed by transfer of the phosphoryl group from EI to HPr. EIIA catalyzes the self-phosphoryl transfer from HPr after which the phosphoryl group is transferred to histidine or cysteine residues of EIIB. The sugar is transported through the membrane-bound EIIC and is phosphorylated by the appropriate sugar-specific EIIB.
Environmental Information Processing; Membrane transport
Phosphotransferase system (PTS)
Polaromonas naphthalenivorans [GN:
phosphoenolpyruvate-protein phosphotransferase; K08483 phosphotransferase system, enzyme I, PtsI [EC:
PTS system fructose subfamily transporter subunit IIA; K02821 PTS system, ascorbate-specific IIA component [EC:
PTS transporter subunit IIA-like nitrogen-regulatory protein PtsN; K02806 PTS system, nitrogen regulatory IIA component [EC:
N-Acetylmuramic acid 6-phosphate
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Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid.
J Bacteriol 186:2385-92 (2004)
Martin-Verstraete I, Debarbouille M, Klier A, Rapoport G
Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon.
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The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis.
Mol Microbiol 47:1353-66 (2003)
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Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor.
J Biol Chem 279:5537-48 (2004)
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EcoCyc: a comprehensive database resource for Escherichia coli.
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J Bacteriol 190:1710-7 (2008)
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Mol Microbiol 37:125-35 (2000)
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The complete phosphotranferase system in Escherichia coli.
J Mol Microbiol Biotechnol 3:329-46 (2001)
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KEGG GENES (3)
All databases (4)
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