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Information on EC 2.7.1.205 - protein-Npi-phosphohistidine-cellobiose phosphotransferase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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protein-Npi-phosphohistidine-cellobiose phosphotransferase
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[protein]-Npi-phospho-L-histidine + cellobiose[side 1] = [protein]-L-histidine + 6-phospho-beta-D-glucosyl-(1.>4)-D-glucose[side 2]
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Starch and sucrose metabolism
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protein-Npi-phospho-L-histidine:cellobiose Npi-phosphotransferase
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
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cellobiose-specific phosphotransferase system
cellobiose-specific PTS permease
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cellobiose-specific PTS system
cellobiose-PTS
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cellobiose-specific phosphotransferase system
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cellobiose-specific phosphotransferase system
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cellobiose-specific PTS system
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cellobiose-specific PTS system
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EIIC
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cellobiose-specific subunit IIC of enzyme II
EIIC
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cellobiose-specific subunit IIC of enzyme II
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ptcBAC
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gene names
PTSCel
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UniProt
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metabolism
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cellobiose transport in L. monocytogenes strain EGD-e is primarily performed by the PTSLac-4 permease and is supported by PTSLac. In the absence of these cellobiose-transporting PTSLac, at least PTSGlc-1 seems to function also as a low-affinity cellobiose transporter
malfunction
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enzyme deletion mutants exhibit reduced virulence
malfunction
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enzyme deletion mutants exhibit reduced virulence
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physiological function
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the enzyme is responsible for biofilm formation and contributes to virulence
physiological function
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the enzyme is responsible for biofilm formation and contributes to virulence
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[protein]-Npi-phospho-L-histidine + 4-methylumbelliferyl-4-D-cellobiopyranoside
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
additional information
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[protein]-Npi-phospho-L-histidine + 4-methylumbelliferyl-4-D-cellobiopyranoside
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[protein]-Npi-phospho-L-histidine + 4-methylumbelliferyl-4-D-cellobiopyranoside
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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additional information
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the cellobiose-specific PTS system is also able to transport lactose
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additional information
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the cellobiose-specific PTS system is also able to transport lactose
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
Q45402
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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[protein]-Npi-phospho-L-histidine + D-cellobiose[side 1]
[protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
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calculated from amino acid sequence
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integral membrane protein
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48805
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x * 48805, calculated from amino acid sequence
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x * 48805, calculated from amino acid sequence
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x * 48805, calculated from amino acid sequence
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Lactococcus lactis LL302 cells
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the gene celB is tightly regulated by the general catabolite repression system and additionally requires the presence of cellobiose to be fully induced
the gene celB is tightly regulated by the general catabolite repression system and additionally requires the presence of cellobiose to be fully induced
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the gene celB is tightly regulated by the general catabolite repression system and additionally requires the presence of cellobiose to be fully induced
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PTEA_BACSU
Bacillus subtilis (strain 168)
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12408
Swiss-Prot
PTEA_GEOSE
108
11785
Swiss-Prot
PTEA_GEOSE
108
11785
Swiss-Prot
PTEB_AERHY
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9716
Swiss-Prot
PTEB_BACSU
Bacillus subtilis (strain 168)
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11443
Swiss-Prot
PTEB_GEOSE
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10737
Swiss-Prot
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Lai, X.; Davis, F.; Hespell, R.; Ingram, L.
Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase genes: Functional expression in recombinant Escherichia coli and identification of a putative binding region for disaccharides
Appl. Environ. Microbiol.
63
355-363
1997
Geobacillus stearothermophilus (Q45402)
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Wu, M.C.; Chen, Y.C.; Lin, T.L.; Hsieh, P.F.; Wang, J.T.
Cellobiose-specific phosphotransferase system of Klebsiella pneumoniae and its importance in biofilm formation and virulence
Infect. Immun.
80
2464-2472
2012
Klebsiella pneumoniae, Klebsiella pneumoniae NTUH-K2044
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Aleksandrzak-Piekarczyk, T.; Polak, J.; Jezierska, B.; Renault, P.; Bardowski, J.
Genetic characterization of the CcpA-dependent, cellobiose-specific PTS system comprising CelB, PtcB and PtcA that transports lactose in Lactococcus lactis IL1403
Int. J. Food Microbiol.
145
186-194
2011
Lactococcus lactis, Lactococcus lactis IL1403
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Lai, X.; Ingram, L.O.
Cloning and sequencing of a cellobiose phosphotransferase system operon from Bacillus stearothermophilus XL-65-6 and functional expression in Escherichia coli
J. Bacteriol.
175
6441-6450
1993
Geobacillus stearothermophilus, Geobacillus stearothermophilus XL-65-6
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Stoll, R.; Goebel, W.
The major PEP-phosphotransferase systems (PTSs) for glucose, mannose and cellobiose of Listeria monocytogenes, and their significance for extra- and intracellular growth
Microbiology
156
1069-1083
2010
Listeria monocytogenes
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Castro, R.; Neves, A.; Fonseca, L.; Pool, W.; Kok, J.; Kuipers, O.; Santos, H.
Characterization of the individual glucose uptake systems of Lactococcus lactis: Mannose-PTS, cellobiose-PTS and the novel GlcU permease
Mol. Microbiol.
71
795-806
2009
Lactococcus lactis, Lactococcus lactis NZ9000
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Reizer, J.; Reizer, A.; Saier Jr., M.
The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus
Res. Microbiol.
141
1061-1067
1990
Escherichia coli
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