Difference between revisions of "Phosphotransferase systems"

From SubtiWiki
Jump to: navigation, search
Line 8: Line 8:
 
* 1.2.3. [[Transporters/ other]]
 
* 1.2.3. [[Transporters/ other]]
 
|Related=
 
|Related=
none
+
* [[PRD-containing transcription factors]]
 +
* [[transport proteins]]
 +
* [[trigger enzymes]]
 
|}}
 
|}}
  
Line 54: Line 56:
 
* [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]
 
* [http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]
 
* [http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism]
 
* [http://subtiwiki.uni-goettingen.de/pathways/carbohydrate_metabolic_pathways.html Sugar catabolism]
 
==Related Lists==
 
* [[PRD-containing transcription factors]]
 
* [[transport proteins]]
 
* [[trigger enzymes]]
 
  
 
==Relevant Reviews==
 
==Relevant Reviews==
 
<pubmed>17158705 9871918 9663674 10627040 11532441 16339738 </pubmed>
 
<pubmed>17158705 9871918 9663674 10627040 11532441 16339738 </pubmed>

Revision as of 11:14, 12 November 2010

Parent categories
Neighbouring categories
Related categories



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

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] [DOI] (P p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[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] [DOI] (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] [DOI] (P p)