Phosphotransferase systems

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The PEP:Sugar Phosphotransferase System

The PTS is a sugar transport system that couples the transport of a sugar to its phosphorylation. The phosphate group is derived from phosphoenolpyruvate (PEP) and transferred via the general PTS proteins Enzyme I (EI) and HPr to the substrate-specific Enzymes II (EII) to the incoming sugars.

In addition to its role in sugar transport, the PTS is also involved in the regulation of carbon metabolism.

General PTS proteins

Sugar specific PTS proteins

  • PtsG: glucose permease, EIICBA
  • GamP: glucosamine permease, EIICBA
  • MurP: N-acetyl muramic acid-specific phosphotransferase system, EIIBC component
  • MtlA, MtlF: mannitol permease
  • GmuA, GmuB, GmuC: galactomannan permease
  • TreP: trehalose permease
  • MalP: maltose permease
  • FruA: fructose permease
  • ManP: mannose permease
  • NagP: N-acetylglucosamine permease, EIICB component
  • LevD, LevE, LevF, LevG: fructose permease
  • SacP: sucrose permease (high affinity)
  • SacY: sucrose permease (low affinity)
  • LicA, LicB, LicC: lichenan permease
  • BglP: ß-glucoside permease
  • YpqE: unknown EIIA component
  • YwbA: unknown EIIC component
  • YyzE: unknown PTS protein

Proteins closely related to the PTS

  • Crh: HPr-like protein with exculsively regulatory functions (His-15 is not conserved
  • HprK: HPr-kinase, key factor for carbon catabolite repression

Non-PTS proteins controlled by PTS-dependent phosphorylation

The PTS in SubtiPathways

Relevant Reviews

Anne Galinier, Josef Deutscher
Sophisticated Regulation of Transcriptional Factors by the Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System.
J. Mol. Biol.: 2017, 429(6);773-789
[PubMed:28202392] [WorldCat.org] [DOI] (I p)

Josef Deutscher, Francine Moussan Désirée Aké, Meriem Derkaoui, Arthur Constant Zébré, Thanh Nguyen Cao, Houda Bouraoui, Takfarinas Kentache, Abdelhamid Mokhtari, Eliane Milohanic, Philippe Joyet
The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.
Microbiol. Mol. Biol. Rev.: 2014, 78(2);231-56
[PubMed:24847021] [WorldCat.org] [DOI] (I p)

Josef Deutscher, Christof Francke, Pieter W Postma
How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
Microbiol. Mol. Biol. Rev.: 2006, 70(4);939-1031
[PubMed:17158705] [WorldCat.org] [DOI] (P p)

Ravi D Barabote, Milton H Saier
Comparative genomic analyses of the bacterial phosphotransferase system.
Microbiol. Mol. Biol. Rev.: 2005, 69(4);608-34
[PubMed:16339738] [WorldCat.org] [DOI] (P p)

C Siebold, K Flükiger, R Beutler, B Erni
Carbohydrate transporters of the bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS).
FEBS Lett.: 2001, 504(3);104-11
[PubMed:11532441] [WorldCat.org] (P p)

J Reizer, S Bachem, A Reizer, M Arnaud, M H Saier, J Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading, Engl.): 1999, 145 ( Pt 12);3419-29
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

J Stülke, W Hillen
Coupling physiology and gene regulation in bacteria: the phosphotransferase sugar uptake system delivers the signals.
Naturwissenschaften: 1998, 85(12);583-92
[PubMed:9871918] [WorldCat.org] (P p)

J Stülke, M Arnaud, G Rapoport, I Martin-Verstraete
PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.
Mol. Microbiol.: 1998, 28(5);865-74
[PubMed:9663674] [WorldCat.org] (P p)


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