Difference between revisions of "Phosphotransferase systems"
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* 1.2.1. [[ABC transporters]] | * 1.2.1. [[ABC transporters]] | ||
* 1.2.2. [[Phosphotransferase systems]] | * 1.2.2. [[Phosphotransferase systems]] | ||
| − | * 1.2.3. [[Transporters/ other]] | + | * 1.2.3. [[ECF transporter]] |
| + | * 1.2.4. [[Transporters/ other]] | ||
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* [[CcpA regulon]] | * [[CcpA regulon]] | ||
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==Relevant Reviews== | ==Relevant Reviews== | ||
| − | <pubmed>17158705 9871918 9663674 10627040 11532441 16339738 </pubmed> | + | <pubmed>17158705 9871918 9663674 10627040 11532441 16339738 24847021 28202392</pubmed> |
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=Back to [[categories]]= | =Back to [[categories]]= | ||
Latest revision as of 14:51, 24 February 2017
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Contents
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
- 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]
[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)
