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Entry
btg02060                    Pathway                                

Name
Phosphotransferase system (PTS) - Bacillus thuringiensis Bt407
Description
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.
Class
Environmental Information Processing; Membrane transport
BRITE hierarchy
Pathway map
btg02060  Phosphotransferase system (PTS)
btg02060

Ortholog table
Module
btg_M00270  PTS system, trehalose-specific II component [PATH:btg02060]
btg_M00273  PTS system, fructose-specific II component [PATH:btg02060]
btg_M00275  PTS system, cellobiose-specific II component [PATH:btg02060]
btg_M00806  PTS system, maltose-specific II component [PATH:btg02060]
btg_M00809  PTS system, glucose-specific II component [PATH:btg02060]
Other DBs
BSID: 700787
GO: 0009401
TC: 4.A
Organism
Bacillus thuringiensis Bt407 [GN:btg]
Gene
BTB_c41830  ptsI; phosphoenolpyruvate-protein phosphotransferase PtsI [KO:K08483] [EC:2.7.3.9]
BTB_c41850  ptsG; PTS system glucose-specific EIICBA component PtsG [KO:K20116 K20117 K20118] [EC:2.7.1.199 2.7.1.199]
BTB_c55210  crr; glucose-specific phosphotransferase enzyme IIA component Crr [KO:K02777] [EC:2.7.1.-]
BTB_c04970  nagP; PTS system N-acetylglucosamine-specific EIICB component NagP [KO:K02803 K02804] [EC:2.7.1.193]
BTB_c04300  exp1; PTS system glucose-specific EIICBA component Exp [KO:K20107 K20108] [EC:2.7.1.208]
BTB_c09100  ybbF; putative PTS system EIIBC component YbbF [KO:K02809 K02810] [EC:2.7.1.211]
BTB_c08440  sacP; PTS system sucrose-specific EIIBC component SacP [KO:K02809 K02810] [EC:2.7.1.211]
BTB_c06450  treP; PTS system trehalose-specific EIIBC component TreP [KO:K02818 K02819] [EC:2.7.1.201]
BTB_c08780  licA1; lichenan-specific phosphotransferase enzyme IIA component LicA [KO:K02759] [EC:2.7.1.205 2.7.1.196]
BTB_c53990  licA2; lichenan-specific phosphotransferase enzyme IIA component LicA [KO:K02759] [EC:2.7.1.205 2.7.1.196]
BTB_c54040  licA3; lichenan-specific phosphotransferase enzyme IIA component LicA [KO:K02759] [EC:2.7.1.205 2.7.1.196]
BTB_c08790  licB1; lichenan-specific phosphotransferase enzyme IIB component LicB [KO:K02760] [EC:2.7.1.205 2.7.1.196]
BTB_c24910  PTS system,diacetylchitobiose-specific IIB component [KO:K02760] [EC:2.7.1.205 2.7.1.196]
BTB_c54010  celA; cellobiose-specific phosphotransferase enzyme IIB component CelA [KO:K02760] [EC:2.7.1.205 2.7.1.196]
BTB_c54060  licB2; lichenan-specific phosphotransferase enzyme IIB component LicB [KO:K02760] [EC:2.7.1.205 2.7.1.196]
BTB_c08800  licC; lichenan permease IIC component LicC [KO:K02761]
BTB_c24920  celB1; cellobiose permease IIC component CelB [KO:K02761]
BTB_c54000  ywbA; putative permease IIC component YwbA [KO:K02761]
BTB_c54050  celB2; cellobiose permease IIC component CelB [KO:K02761]
BTB_c37880  fruA; PTS system fructose-specific EIIABC component FruA [KO:K02768 K02769 K02770] [EC:2.7.1.202 2.7.1.202]
BTB_c54600  manP; PTS system mannose-specific EIIBCA component ManP [KO:K02768 K02769 K02770] [EC:2.7.1.202 2.7.1.202]
Compound
C00022  Pyruvate
C00031  D-Glucose
C00072  Ascorbate
C00074  Phosphoenolpyruvate
C00089  Sucrose
C00092  D-Glucose 6-phosphate
C00095  D-Fructose
C00124  D-Galactose
C00140  N-Acetyl-D-glucosamine
C00159  D-Mannose
C00185  Cellobiose
C00208  Maltose
C00243  Lactose
C00275  D-Mannose 6-phosphate
C00329  D-Glucosamine
C00352  D-Glucosamine 6-phosphate
C00357  N-Acetyl-D-glucosamine 6-phosphate
C00392  Mannitol
C00644  D-Mannitol 1-phosphate
C00689  alpha,alpha'-Trehalose 6-phosphate
C00697  Nitrogen
C00794  D-Sorbitol
C01083  alpha,alpha-Trehalose
C01094  D-Fructose 1-phosphate
C01096  Sorbitol 6-phosphate
C01113  D-Galactose 6-phosphate
C01132  N-Acetyl-D-galactosamine
C01451  Salicin
C01452  Sorbose
C01674  Chitobiose
C01697  Galactitol
C01798  D-Glucoside
C02262  D-Galactosamine
C02713  N-Acetylmuramate
C02888  Sorbose 1-phosphate
C02995  Maltose 6'-phosphate
C03752  2-Amino-2-deoxy-D-gluconate
C04534  6-Phospho-beta-D-glucosyl-(1,4)-D-glucose
C05396  Lactose 6'-phosphate
C06186  Arbutin
C06187  Arbutin 6-phosphate
C06188  Salicin 6-phosphate
C06311  Galactitol 1-phosphate
C06376  N-Acetyl-D-galactosamine 6-phosphate
C06377  D-Galactosamine 6-phosphate
C11544  2-O-(alpha-D-Mannosyl)-D-glycerate
C16186  L-Ascorbate 6-phosphate
C16488  Fructoselysine
C16489  Fructoselysine 6-phosphate
C16688  Sucrose 6-phosphate
C16698  N-Acetylmuramic acid 6-phosphate
C16699  2-O-(6-Phospho-alpha-mannosyl)-D-glycerate
C20589  D-Glucosaminate-6-phosphate
C20978  Glucoselysine
C20979  Glucoselysine-6-phosphate
C21152  N,N'-Diacetylchitobiose 6'-phosphate
Reference
  Authors
Darbon E, Galinier A, Le Coq D, Deutscher J.
  Title
Phosphotransfer functions mutated Bacillus subtilis HPr-like protein Crh carrying a histidine in the active site.
  Journal
J Mol Microbiol Biotechnol 3:439-44 (2001)
Reference
  Authors
Dahl U, Jaeger T, Nguyen BT, Sattler JM, Mayer C.
  Title
Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid.
  Journal
J Bacteriol 186:2385-92 (2004)
DOI:10.1128/JB.186.8.2385-2392.2004
Reference
PMID:2117666
  Authors
Martin-Verstraete I, Debarbouille M, Klier A, Rapoport G
  Title
Levanase operon of Bacillus subtilis includes a fructose-specific phosphotransferase system regulating the expression of the operon.
  Journal
J Mol Biol 214:657-71 (1990)
DOI:10.1016/0022-2836(90)90284-S
Reference
  Authors
Kristich CJ, Glekas GD, Ordal GW.
  Title
The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis.
  Journal
Mol Microbiol 47:1353-66 (2003)
DOI:10.1046/j.1365-2958.2003.03375.x
Reference
  Authors
Sampaio MM, Chevance F, Dippel R, Eppler T, Schlegel A, Boos W, Lu YJ, Rock CO.
  Title
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.
  Journal
J Biol Chem 279:5537-48 (2004)
DOI:10.1074/jbc.M310980200
Reference
  Authors
Keseler IM, Collado-Vides J, Gama-Castro S, Ingraham J, Paley S, Paulsen IT, Peralta-Gil M, Karp PD.
  Title
EcoCyc: a comprehensive database resource for Escherichia coli.
  Journal
Nucleic Acids Res 33:D334-7 (2005)
DOI:10.1093/nar/gki108
Reference
  Authors
Mukherjee A, Mammel MK, LeClerc JE, Cebula TA.
  Title
Altered utilization of N-acetyl-D-galactosamine by Escherichia coli O157:H7 from the 2006 spinach outbreak.
  Journal
J Bacteriol 190:1710-7 (2008)
DOI:10.1128/JB.01737-07
Reference
  Authors
Brinkkotter A, Kloss H, Alpert C, Lengeler JW.
  Title
Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli.
  Journal
Mol Microbiol 37:125-35 (2000)
DOI:10.1046/j.1365-2958.2000.01969.x
Reference
  Authors
Tchieu JH, Norris V, Edwards JS, Saier MH Jr.
  Title
The complete phosphotranferase system in Escherichia coli.
  Journal
J Mol Microbiol Biotechnol 3:329-46 (2001)
Reference
  Authors
Kotrba P, Inui M, Yukawa H.
  Title
Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism.
  Journal
J Biosci Bioeng 92:502-17 (2001)
DOI:10.1016/S1389-1723(01)80308-X
KO pathway
ko02060   

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