Subsystem: Trehalose Uptake and Utilization

This subsystem's description is:

Trehalose (alpha-D-glucopyranosyl-alpha-D-glucopyranoside) is a non-reducing disaccharide that has been found in many organisms able to withstand almost complete desiccation, including bacteria, fungi, protozoa, plants and invertebrates.
Trehalose serves as storage carbohydrate and is one of the most effective substances, known to protect membranes against the deleterious effects of dehydration, most likely by interaction of the hydroxyl groups of trehalose with the phosphate head groups of the phospholipids.

=====VARIANTS:====================

1.0 – organisms possessing the trehalose uptake and utilization system;
1.x – missing gene in the pathway of trehalose uptake and utilization;
2.0 – Shewanella-like trehalose uptake and utilization system: TreA+treP+omp_tre+treR-II;
3.0 - Putative_Trehalose_utilization_system;
4.0 - Utilization only - organisms have both PGM and TP but missing a transporter;

-1 – no pathway in this organism;
0 – variant is not determined yet.

For more information, please check out the description and the additional notes tabs, below

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Taxonomy Pattern 
Organism 
Domain
Variant [?] 
active
*TreRTreT*PTS_TreTreCTreATreFMalAPGMTPTPPLamBGlcPomp_tre*trePtreR-IIICP*PTS_Glu*TreXYZ
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Trehalose (alpha-D-glucopyranosyl-alpha-D-glucopyranoside) is a non-reducing disaccharide that has been found in many organisms able to withstand almost complete desiccation, including bacteria, fungi, protozoa, plants and invertebrates.
Trehalose serves as storage carbohydrate and is one of the most effective substances, known to protect membranes against the deleterious effects of dehydration, most likely by interaction of the hydroxyl groups of trehalose with the phosphate head groups of the phospholipids.

=====VARIANTS:====================

1.0 – organisms possessing the trehalose uptake and utilization system;
1.x – missing gene in the pathway of trehalose uptake and utilization;
2.0 – Shewanella-like trehalose uptake and utilization system: TreA+treP+omp_tre+treR-II;
3.0 - Putative_Trehalose_utilization_system;
4.0 - Utilization only - organisms have both PGM and TP but missing a transporter;

-1 – no pathway in this organism;
0 – variant is not determined yet.
Active uptake systems for trehalose have been characterized in E. coli, Vibrio parahaemolyticus and Bacillus subtilis, acting as phosphoenolpyruvate sugar phosphotransferase (PTS) transporters, whereas in S. cerevisiae an H+-trehalose symporter has been described.
In the hyperthermophilic archaeon Thermococcus litoralis a binding protein-dependent ABC transporter for trehalose and maltose has recently been identified. The family of prokaryotic-binding protein-dependent ABC transport systems comprise two membrane proteins, forming the permeases, a dimeric ATP-binding protein and a substrate-binding protein located outside the cytoplasmic membrane. Contrary to Gram-negative bacteria, in Gram-positive and archaea bacteria the substrate-binding proteins are anchored by their lipidated N-terminus.

L. acidophilus NCFM has the ability to utilize trehalose as a primary carbohydrate source using a PTS transporter and carbohydrate hydrolase encoded within the genome.

In E. coli and B. subtilis, trehalose has been shown to be transported by a PTS, which translocates and phosphorylates trehalose via a specific EIICB-Tre and the EIIA-Glc of the glucose-PTS releasing trehalose-6-phosphate into the cell.
In L. acidophilus NCFM, trehalose appears to be transported by an EIIABC-Tre rather than by EIICB-Tre and EIIA-Glc. Based on genomic content, all of the trehalose-fermenting lactic acid bacteria available in the public database appear to utilize trehalose in a similar manner.

The resulting trehalose-6-phosphate is then subsequently hydrolyzed into glucose and glucose-6-phosphate by a trehalose-6-phosphate hydrolase (EC 3.2.1.93); these products can be used as substrates for glycolysis.

---------------Glucose uptake in B.subtilis:--------------------

Bacillus subtilis has at least three different pathways for glucose uptake. The first is the glucose-specific phosphoenolpyruvate-dependent phosphotransferase system (glucose-PTS), which is widespread among bacteria and plays an essential role in both the transport and the phosphorylation of glucose. Encoded by the ptsGHI operon, glucose-PTS is the predominant glucose uptake pathway of B. subtilis and promotes carbon catabolite regulation mediated by a master transcriptional regulator, CcpA.
The remaining two pathways are the non-PTS-type transporters GlcP and GlcU.
GlcP is a proton-dependent glucose/mannose symport permease and a member of the major facilitator superfamily. It's shown that cells lacking functional GlcP import 30% less glucose than wild-type cells and that GlcP contributes partially to glucose-promoted catabolite repression. The gene encoding GlcU and a downstream gdh gene encoding glucose dehydrogenase form an operon that is transcribed in forespores after the onset of sporulation. Thus, GlcU probably functions in forespores during sporulation or in germinating spores rather than in vegetative cells.

*********REFERENSES:**********************

1. Andersson U, Levander F, Radstrom P. Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. J Biol Chem. 2001 Nov 16;276(46):42707-13. PMID: 11553642.

2. Barrangou R, Azcarate-Peril MA, Duong T, Conners SB, Kelly RM, Klaenhammer TR. Global analysis of carbohydrate utilization by Lactobacillus acidophilus using cDNA microarrays. Proc Natl Acad Sci U S A. 2006 Feb 27; PMID: 16505367.

3. T. Duong, R. Barrangou, W. M. Russell, and T. R. Klaenhammer
Characterization of the tre Locus and Analysis of Trehalose Cryoprotection in Lactobacillus acidophilus NCFM. Appl. Envir. Microbiol., February 1, 2006; 72(2): 1218 - 1225.

4. Schlosser, A. 2000. MsiK-dependent trehalose uptake in Streptomyces reticuli. FEMS Microbiol. Lett. 184:187-192.

5. Silva Z, Sampaio MM, Henne A, Bohm A, Gutzat R, Boos W, da Costa MS, Santos H. The high-affinity maltose/trehalose ABC transporter in the extremely thermophilic bacterium Thermus thermophilus HB27 also recognizes sucrose and palatinose. J Bacteriol. 2005 Feb;187(4):1210-8. PMID: 15687184

6. del Castillo, T., E. Duque, and J.L. Ramos. (2008). A set of activators and repressors control peripheral glucose pathways in Pseudomonas putida to yield a common central intermediate. J. Bacteriol. 190: 2331-2339.PMID:18245293

6a. del Castillo, T., J. L. Ramos, J. J. Rodrνguez-Herva, T. Fuhrer, U. Sauer, and E. Duque. 2007. Convergent peripheral pathways catalyze initial glucose catabolism in Pseudomonas putida: genomic and flux analysis. J. Bacteriol. 189:5142-5152.

Currently selected organism: none (open scenarios overview page)