EC Number   |
General Information |
Reference |
|---|
   7.6.2.10 | evolution |
conservation of the signature residues of UgpB proteins, Sec- and Tat-specific signal peptides vary in their length because of different properties associated with them, Sec-predicted UgpB proteins contain a shorter signal peptide compared to Tat-specific, overview |
-, 751465 |
| 7.6.2.10 | evolution |
conservation of the signature residues of UgpB proteins, Sec- and Tat-specific signal peptides vary in their length because of different properties associated with them, Sec-predicted UgpB proteins contain a shorter signal peptide compared to Tat-specific, overview. The majority of UgpB proteins have Sec-specific tripartite structure in their signal peptide. Sec-predicted UgpB proteins contain highly hydrophobic h-region of the tripartite structure |
-, 751465 |
| 7.6.2.10 | evolution |
the enzymes are members of the G3Pp family, lack of functional redundancy in the gene family, and differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview |
-, 720742 |
| 7.6.2.10 | malfunction |
in Staphylococcus aureus, plasmid overexpression of the Tet38 efflux pump and a glpT mutant result in increased MICs and decreased accumulation of fosfomycin, with MICs affected by glycerol-3-phosphate. In contrast, a tet38 mutant has a lower MIC and increases accumulation of fosfomycin, suggesting that Tet38 acts as an efflux transporter of fosfomycin |
-, 749596 |
| 7.6.2.10 | metabolism |
two transport systems (Glp and Ugp) associated with transport of deacylated product such as sn-glycerol-3-phosphate (G3P) and glycerophosphodiester are located in the inner membrane, overview |
-, 750690 |
| 7.6.2.10 | more |
fosfomycin is widely used to treat urinary tract and pediatric gastrointestinal infections of bacteria. It is supposed that this antibiotic enters cells via two transport systems, including the bacterial glycerol-3-phosphate transporter, GlpT. Impaired function of GlpT is one mechanism for fosfomycin resistance. Interaction of fosfomycin with the recombinant and purified GlpT of Escherichia coli reconstituted in liposomes, overview |
718976 |
| 7.6.2.10 | more |
protein UgpB three-dimensional structure comparison with the Thermus thermophilus sugar ABC transporter periplasmic sugar-binding protein |
-, 750690 |
| 7.6.2.10 | physiological function |
GlpT is a transporter for glycerol-3-phosphate (G3P) uptake. It also transports the antimicrobial agent and MurA inhibitor fosfomycin. The physiological substrate of GlpT, glycerol-3-phosphate, weakly inhibits the uptake of fosfomycin. The addition of G3P also affects tet38-mediated resistance to two other substrates in addition to fosfomycin. The Tet38 efflux pump is the main transporter for fosfomycin |
-, 749596 |
| 7.6.2.10 | physiological function |
oxygen limitation enhances the antimicrobial activity of fosfomycin in Pseudomonas aeruginosa following overexpression of glpT which encodes glycerol-3-phosphate/fosfomycin symporter. Glycerol-3-phosphate is a native substrate of GlpT transporter, and it is a sole carbon source for growth. Cells grown anaerobically exhibit a higher expression of glpT encoding a glycerol-3-phosphate transporter which is responsible for fosfomycin uptake, causing increased intracellular accumulation of the drug. Increased GlpT expression is due to activation by ANR, resulting in increased uptake of the drug fosfomycin leading to increased antibacterial activity. GlpT is only the transporter for fosfomycin uptake in Pseudomonas aeruginosa since it lacks the uhpT gene. Apart from GlpT, Pseudomonas aeruginosa produces chromosomally encoded FosA that confers innate tolerance by inactivating fosfomycin. Fosfomycin is more active under anaerobic conditions to not only strain PAO1 but also the clinical isolate Ps.a-682 |
-, 750644 |
| 7.6.2.10 | physiological function |
oxygen limitation enhances the antimicrobial activity of fosfomycin in Pseudomonas aeruginosa following overexpression of glpT which encodes glycerol-3-phosphate/fosfomycin symporter. The clinical isolate Ps.a-682 exhibits a promoted biofilm phenotype. Glycerol-3-phosphate is a native substrate of GlpT transporter, and it is a sole carbon source for growth. Cells grown anaerobically exhibit a higher expression of glpT encoding a glycerol-3-phosphate transporter which is responsible for fosfomycin uptake, causing increased intracellular accumulation of the drug. Increased GlpT expression is due to activation by ANR, resulting in increased uptake of the drug fosfomycin leading to increased antibacterial activity. GlpT is only the transporter for fosfomycin uptake in Pseudomonas aeruginosa since it lacks the uhpT gene. Apart from GlpT, Pseudomonas aeruginosa produces chromosomally encoded FosA that confers innate tolerance by inactivating fosfomycin. Fosfomycin is more active under anaerobic conditions to not only strain PAO1 but also the clinical isolate Ps.a-682 |
750644 |
