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Information on EC 7.6.2.10 - ABC-type glycerol 3-phosphate transporter
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EC Tree
7.6.2.10 ABC-type glycerol 3-phosphate transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.
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Word Map
- 7.6.2.10
- fosmidomycin
- reductoisomerase
-
rocker-switch
- methylerythritol
- 1-deoxy-d-xylulose
-
proton-coupled
- glycerophosphocholine
- glycerophosphodiester
-
six-helix
-
alternating-access
-
substrate-translocation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
=
+
+
+
+
+
sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
=
+
+
+
[glycerol 3-phosphate-binding protein][side 1]
Synonyms
glycerol-3-phosphate transporter, glpt transporter, glycerol 3-phosphate transporter, ugpabce transporter, ugpabce, sn-glycerol-3-phosphate transporter, g3p transporter, glycerol-3-phosphate permease, sn-glycerol-3-phosphate-binding periplasmic protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.6.3.20
-
-
formerly
-
G3Pp
GlpT
GlpT transporter
glycerol-3-phosphate permease
glycerol-3-phosphate transporter
glycerol-3-phosphate-transporting ATPase
-
-
-
-
glycerol-3-phosphate/fosfomycin symporter
PA5235
sn-glycerol-3-phosphate transport system permease
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
sn-glycerol-3-phosphate transport system permease protein
sn-glycerol-3-phosphate transport system permease protein upgA
-
-
-
-
sn-glycerol-3-phosphate transport system permease protein upgE
-
-
-
-
sn-glycerol-3-phosphate-binding periplasmic protein
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
TTHN1_01087
UgpA
UgpABCE
ugpB
additional information
sn-glycerol-3-phosphate transport system permease protein
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
sn-glycerol-3-phosphate transport system permease protein
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
sn-glycerol-3-phosphate transport system permease protein
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
additional information
-
the enzyme belongs to the major facilitator MFS transporter superfamily
additional information
-
the enzyme belongs to the major facilitator MFS transporter superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1] = ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, sn-glycerol 3-phosphate-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + glycerol-3-phosphocholine/out
ADP + phosphate + glycerol-3-phosphocholine/in
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
-
-
-
?
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
-
-
?
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
-
-
?
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
phosphate-limitation inducible uptake system for sn-glycerol-3-phosphate
-
-
?
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
-
-
-
?
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
additional information
?
-
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
-
GlpT is responsible for secondary active transport of substrate across the cell membrane, which is crucial to many cellular and physiological processes, overview
-
-
?
additional information
?
-
-
mechanism for substrate translocation across the membrane that involves a rocker-switch-type movement of the protein, transport assays at different conditions using whole cells or purified enzyme, overview
-
-
?
additional information
?
-
-
GltP is an organic phosphate/inorganic phosphate antiporter
-
-
?
additional information
?
-
-
the enzyme performs G3P/G3P exchange, it shows virtually poor exchange activity using phosphoenolpyruvate, fosfomycin and sulphate, and no activity with glutamate, glutamine, aspartate and ATP. Highest activity in the presence of internal glycerol-3-phosphate and phosphate
-
-
?
additional information
?
-
glycerol-2-phosphate is not a substrate
-
-
?
additional information
?
-
-
a major conformational switching mechanism accounts for ligand transport by MFS proteins
-
-
?
additional information
?
-
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the Thermus thermophilus UgpB also transports glycerophosphocholine
-
-
?
additional information
?
-
the Thermus thermophilus UgpB also transports glycerophosphocholine
-
-
?
additional information
?
-
the Thermus thermophilus UgpB also transports glycerophosphocholine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
-
-
?
ATP + H2O + glycerol-3-phosphate/out
ADP + phosphate + glycerol-3-phosphate/in
-
phosphate-limitation inducible uptake system for sn-glycerol-3-phosphate
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
A0A3P4ARZ2; A0A3P4AR76; G9MB86
-
-
-
?
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
-
-
-
?
additional information
?
-
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
GlPt mediates the exchange of glycerol-3-phosphate and phosphate across the membrane
-
-
?
additional information
?
-
-
GlpT is responsible for secondary active transport of substrate across the cell membrane, which is crucial to many cellular and physiological processes, overview
-
-
?
additional information
?
-
-
GltP is an organic phosphate/inorganic phosphate antiporter
-
-
?
additional information
?
-
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
-
the GlpT transporter also transports fosfomycin
-
-
?
additional information
?
-
the GlpT transporter also transports fosfomycin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fosfomycin
-
fosfomycin, externally added to the proteoliposomes, poorly inhibits the glycerol-3-phosphate/glycerol-3-phosphate antiport catalyzed by the reconstituted transporter, completely competitive, interaction of fosfomycin with the recombinant and purified GlpT of Escherichia coli reconstituted in liposomes, overview
additional information
not inhibited by phosphate or by the signal transducing protein PhoU or the phosphodiesterase UgpQ
-
additional information
-
not inhibited by phosphate or by the signal transducing protein PhoU or the phosphodiesterase UgpQ
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Structural analysis of Mycobacterium tuberculosis ATP-binding cassette transporter subunit UgpB reveals specificity for glycerophosphocholine.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, rocker-switch mechanism of membrane transport by GlpT, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.4
fosfomycin
Escherichia coli
-
externally added to the proteoliposomes with reconstituted transporter, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme complex components encoded by genes ugpA_1, ugpB, and ugpE
A0A3P4ARZ2; A0A3P4AR76; G9MB86
UniProt
brenda
enzyme complex components encoded by genes ugpA_1, ugpB, and ugpE
A0A3P4ARZ2; A0A3P4AR76; G9MB86
UniProt
brenda
enzyme complex components encoded by genes ugpA_1, ugpB, and ugpE
A0A3P4ARZ2; A0A3P4AR76; G9MB86
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
brenda
additional information
differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
brenda
additional information
differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
brenda
additional information
differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
brenda
additional information
differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
brenda
additional information
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differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme contains 12-transmembrane alpha-helices which form two domains, each of six transmembrane helices, surrounding a central lingand-binding cavity
brenda
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the enzyme contains 12-transmembrane alpha-helical topologies with two six-helix halves connected by a long loop
brenda
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probable an integral membrane protein
brenda
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probable an integral membrane protein
-
brenda
additional information
Escherichia coli (EcUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
brenda
additional information
UgpB protein from Mycobacterium tuberculosis (MtUgpB) follows the Tat pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
brenda
additional information
-
UgpB protein from Mycobacterium tuberculosis (MtUgpB) follows the Tat pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
-
brenda
additional information
Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
brenda
additional information
-
Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
-
brenda
additional information
-
Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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
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
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
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
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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
-
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
-
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
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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
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
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metabolism
A0A3P4ARZ2; A0A3P4AR76; G9MB86
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
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
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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
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physiological function
the glycerol-3-phosphate transporter is a sugar phosphate/anion antiporter also implicated in phosphate mobilization. G3Pps have a role during seedling growth in Arabidopsis thaliana
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
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
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
physiological function
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. Mycobacterium tuberculosis UgpB protein is crucial for its optimal growth. UgpB protein from Mycobacterium tuberculosis (MtUgpB) follows the Tat pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview
physiological function
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. UgpB protein from Escherichia coli (EcUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway or the Sec pathway, overview
physiological function
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. UgpB protein from Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview
physiological function
A0A3P4ARZ2; A0A3P4AR76; G9MB86
the enzyme complex UgpABCE is a ATP-binding cassette (ABC) transporter for sn-glycerol-3-phosphate (G3P). UgpA and UgpE constitute the transmembrane domains (TMDs), UgpC forms the dimer of ATP-hydrolyzing component, and UgpB is the periplasmic substrate binding protein
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
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physiological function
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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
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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
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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
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physiological function
-
the enzyme complex UgpABCE is a ATP-binding cassette (ABC) transporter for sn-glycerol-3-phosphate (G3P). UgpA and UgpE constitute the transmembrane domains (TMDs), UgpC forms the dimer of ATP-hydrolyzing component, and UgpB is the periplasmic substrate binding protein
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physiological function
-
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. UgpB protein from Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview
-
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
-
physiological function
-
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. Mycobacterium tuberculosis UgpB protein is crucial for its optimal growth. UgpB protein from Mycobacterium tuberculosis (MtUgpB) follows the Tat pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview
-
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
-
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
-
physiological function
-
the glycerol-3-phosphate transporter is a sugar phosphate/anion antiporter also implicated in phosphate mobilization. G3Pps have a role during seedling growth in Arabidopsis thaliana
-
physiological function
-
the enzyme complex UgpABCE is a ATP-binding cassette (ABC) transporter for sn-glycerol-3-phosphate (G3P). UgpA and UgpE constitute the transmembrane domains (TMDs), UgpC forms the dimer of ATP-hydrolyzing component, and UgpB is the periplasmic substrate binding protein
-
physiological function
-
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. UgpB protein from Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview
-
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
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additional information
-
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
additional information
A0A3P4ARZ2; A0A3P4AR76; G9MB86
protein UgpB three-dimensional structure comparison with the Thermus thermophilus sugar ABC transporter periplasmic sugar-binding protein
additional information
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protein UgpB three-dimensional structure comparison with the Thermus thermophilus sugar ABC transporter periplasmic sugar-binding protein
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additional information
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protein UgpB three-dimensional structure comparison with the Thermus thermophilus sugar ABC transporter periplasmic sugar-binding protein
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Show AA Sequence and Transmembrane Helices (3406 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
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the enzyme contains 12 highly flexible transmembrane alpha-helices, H1-H12, which form two domains, each of six transmembrane helices, surrounding a central lingand-binding cavity, molecular dynamic simulations and modelling, comparison of conformational properties with other MFS family members, overview
additional information
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interdomain interaction analysis and enzyme structure modelling, steered molecular dynamics simulation, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
additional information
UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
additional information
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UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
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additional information
UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
additional information
-
UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
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additional information
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UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with glycerol-3-phosphate, sitting drop vapor diffusion method, using 5 mM CoCl3, 5 mM NiCl2, 5 mM CdCl2, 5 mM MgCl2, 0.1 M HEPES, pH 7.5, 12% (w/v) polyethylene glycol 3350, and 0.3% octyl-beta-D-glucopyranoside
X-ray structure, GlpT consists of 12 transmembrane helices, which form a N- and C-terminal domain, the structure reveals a large internal cavity, open toward the cytoplasm but completely closed to the periplasm, the substrate-binding site, formed by two arginine residues, is accessible from only one side of the membrane at a time
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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generation of a AtG3Pp4 knockdown mutant, phenotype, overview
additional information
generation of a AtG3Pp4 knockdown mutant, phenotype, overview
additional information
generation of a AtG3Pp4 knockdown mutant, phenotype, overview
additional information
generation of a AtG3Pp4 knockdown mutant, phenotype, overview
additional information
generation of a AtG3Pp4 knockdown mutant, phenotype, overview
additional information
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generation of a AtG3Pp4 knockdown mutant, phenotype, overview
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additional information
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GlpT appears to operate via a single binding-site, alternating-acess mechanism
additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
additional information
construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
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construction of an in-frame deletion of glpT in PAO1 background, PAO1DELTAglpT
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additional information
construction of mutant strain QT03 (glpT::Tn) by phage phi85 transduction using the Staphylococcus aureus donor USA300 (glpT::Tn) and RN6390 as a recipient
additional information
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construction of mutant strain QT03 (glpT::Tn) by phage phi85 transduction using the Staphylococcus aureus donor USA300 (glpT::Tn) and RN6390 as a recipient
additional information
-
construction of mutant strain QT03 (glpT::Tn) by phage phi85 transduction using the Staphylococcus aureus donor USA300 (glpT::Tn) and RN6390 as a recipient
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme 55fold from Escherichia coli strain SH116 by nickel affinity chromatography
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recombinant His-tagged wild-type enzyme from mutant GlpT-deficient strain SH1200 by ultracentrifugation and nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ArG3Pp3, cloning of 5 genes encoding G3Pps, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis. Differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
gene AtG3Pp1, cloning of 5 genes encoding G3Pps, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis. Differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
gene AtG3Pp2, cloning of 5 genes encoding G3Pps, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis. Differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
gene AtG3Pp4, cloning of 5 genes encoding G3Pps, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis. Differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
gene AtG3Pp5, cloning of 5 genes encoding G3Pps, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis. Differential expression patterns of the promoter-GUS fusion transgenics for the G3Pp gene family during seedling growth, overview
gene glpT, recombinant expression in Staphylococcus aureus, plasmids pLI50-glpT and pLI50-tet38 are first constructed in Escherichia coli TOP10 cells and then reintroduced into Staphlyococcus aureus strains RN4220 and 6390
gene glpT, sequence comparisons with ANR binding site and glpT transcriptional start site, construction of lacZ reporter plasmids to measure promoter activities of glpT in PAO1 and Ps.a-682, and fosA and glpR in PAO1, designated pBBRglpT(PAO1)-P, pBBRglpT(Ps.a-682)-P, pBBRfosA(PAO1)-P, and pBBRglpR(PAO1)-P, respectively
gene ugpB, sequence comparisons and phylogenetic analysis
operon UgpABCE, sequence comparisons and phylogenetic tree
A0A3P4ARZ2; A0A3P4AR76; G9MB86
overexpression of His-tagged wild-type enzyme in mutant GlpT-deficient strain SH1200
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene AtG3Pp1 is induced 24fold in the roots of phosphate-deprived seedlings
gene AtG3Pp2 is induced 3fold in the roots of phosphate-deprived seedlings
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
phosphate deficiency-mediated induction of AtG3Pp4 is evident in both roots and shoots
phosphate deficiency-mediated induction of gene AtG3Pp3 is evident in both roots and shoots
gene AtG3Pp1 is induced 24fold in the roots of phosphate-deprived seedlings
gene AtG3Pp1 is induced 24fold in the roots of phosphate-deprived seedlings
-
-
gene AtG3Pp2 is induced 3fold in the roots of phosphate-deprived seedlings
gene AtG3Pp2 is induced 3fold in the roots of phosphate-deprived seedlings
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
GlpR is a repressor for the glpT gene expression, no significant difference in glpR expression between both conditions, aerobic and anaerobic growth
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
oxygen limitation leads to overexpression in Pseudomonas aeruginosa. Anaerobic regulator protein ANR is an activator of glpT gene expression, it binds to the DNA fragment from glpT region upstream
-
-
phosphate deficiency-mediated induction of AtG3Pp4 is evident in both roots and shoots
phosphate deficiency-mediated induction of AtG3Pp4 is evident in both roots and shoots
-
-
phosphate deficiency-mediated induction of gene AtG3Pp3 is evident in both roots and shoots
phosphate deficiency-mediated induction of gene AtG3Pp3 is evident in both roots and shoots
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bahl, H.; Burchardt, G.; Wienecke, A.
Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding-protein-dependent transport systems
FEMS Microbiol. Lett.
65
83-87
1991
Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1
brenda
Overduin, P.; Boos, W.; Tomassen, J.
Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to the maltose system
Mol. Microbiol.
2
767-775
1988
Escherichia coli
brenda
Sofia, H.J.; Burland, V.; Daniels, D.L.; Plunkett, G.3rd.; Blattner, F.R.
Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes
Nucleic Acids Res.
22
2576-2586
1994
Escherichia coli (P10905), Escherichia coli (P10906)
brenda
Abramson, J.; Kaback, H.R.; Iwata, S.
Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: members of the major facilitator superfamily
Curr. Opin. Struct. Biol.
14
413-419
2004
Escherichia coli
brenda
Lemieux, M.J.; Huang, Y.; Wang, D.N.
Crystal structure and mechanism of GlpT, the glycerol-3-phosphate transporter from E. coli
J. Electron Microsc. (Tokyo)
54
i43-i46
2005
Escherichia coli
brenda
Law, C.J.; Yang, Q.; Soudant, C.; Maloney, P.C.; Wang, D.N.
Kinetic evidence is consistent with the rocker-switch mechanism of membrane transport by GlpT
Biochemistry
46
12190-12197
2007
Escherichia coli
brenda
Tsigelny, I.F.; Greenberg, J.; Kouznetsova, V.; Nigam, S.K.
Modeling of glycerol-3-phosphate transporter suggests a potential tilt mechanism involved in its function
J. Bioinform. Comput. Biol.
6
885-904
2008
Homo sapiens
brenda
D'Rozario, R.S.; Sansom, M.S.
Helix dynamics in a membrane transport protein: comparative simulations of the glycerol-3-phosphate transporter and its constituent helices
Mol. Membr. Biol.
25
571-583
2008
Escherichia coli
brenda
Santoro, A.; Cappello, A.R.; Madeo, M.; Martello, E.; Iacopetta, D.; Dolce, V.
Interaction of fosfomycin with the glycerol 3-phosphate transporter of Escherichia coli
Biochim. Biophys. Acta
1810
1323-1329
2011
Escherichia coli
brenda
Ramaiah, M.; Jain, A.; Baldwin, J.C.; Karthikeyan, A.S.; Raghothama, K.G.
Characterization of the phosphate starvation-induced glycerol-3-phosphate permease gene family in Arabidopsis
Plant Physiol.
157
279-291
2011
Arabidopsis thaliana, Arabidopsis thaliana (O23596), Arabidopsis thaliana (Q9C5L3), Arabidopsis thaliana (Q9SA71), Arabidopsis thaliana (Q9SB41), Arabidopsis thaliana Columbia, Arabidopsis thaliana Columbia (O23596), Arabidopsis thaliana Columbia (Q9C5L3), Arabidopsis thaliana Columbia (Q9SA71), Arabidopsis thaliana Columbia (Q9SB41)
brenda
Wuttge, S.; Bommer, M.; Jaeger, F.; Martins, B.M.; Jacob, S.; Licht, A.; Scheffel, F.; Dobbek, H.; Schneider, E.
Determinants of substrate specificity and biochemical properties of the sn-glycerol-3-phosphate ATP binding cassette transporter (UgpB-AEC2) of Escherichia coli
Mol. Microbiol.
86
908-920
2012
Escherichia coli (P0AG80), Escherichia coli
brenda
Truong-Bolduc, Q.C.; Wang, Y.; Hooper, D.C.
Tet38 efflux pump contributes to fosfomycin resistance in Staphylococcus aureus
Antimicrob. Agents Chemother.
62
e00927-18
2018
Staphylococcus aureus (A0A0H3JLD7), Staphylococcus aureus, Staphylococcus aureus N315 (A0A0H3JLD7)
brenda
Hirakawa, H.; Kurabayashi, K.; Tanimoto, K.; Tomita, H.
Oxygen limitation enhances the antimicrobial activity of fosfomycin in Pseudomonas aeruginosa following overexpression of glpT which encodes glycerol-3-phosphate/fosfomycin symporter
Front. Microbiol.
9
1950
2018
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HTV5), Pseudomonas aeruginosa ATCC 15692 (Q9HTV5), Pseudomonas aeruginosa 1C (Q9HTV5), Pseudomonas aeruginosa PRS 101 (Q9HTV5), Pseudomonas aeruginosa DSM 22644 (Q9HTV5), Pseudomonas aeruginosa CIP 104116 (Q9HTV5), Pseudomonas aeruginosa LMG 12228 (Q9HTV5), Pseudomonas aeruginosa JCM 14847 (Q9HTV5)
brenda
Chandravanshi, M.; Gogoi, P.; Kanaujia, S.P.
Computational characterization of TTHA0379 a potential glycerophosphocholine binding protein of Ugp ATP-binding cassette transporter
Gene
592
260-268
2016
Thermus thermophilus (A0A3P4ARZ2 AND A0A3P4AR76 AND G9MB86), Thermus thermophilus DSM 579 (A0A3P4ARZ2 AND A0A3P4AR76 AND G9MB86), Thermus thermophilus ATCC 27634 (A0A3P4ARZ2 AND A0A3P4AR76 AND G9MB86)
brenda
Adhikari, R.; Singh, D.; Chandravanshi, M.; Dutta, A.; Kanaujia, S.
UgpB, a periplasmic component of the UgpABCE ATP-binding cassette transporter, predominantly follows the Sec translocation pathway
Meta Gene
13
129-139
2017
Mycobacterium tuberculosis (A5U6I5), Escherichia coli (P0AG80), Thermus thermophilus (Q5SLB4), Thermus thermophilus DSM 579 (Q5SLB4), Mycobacterium tuberculosis ATCC 25177 (A5U6I5), Thermus thermophilus ATCC 27634 (Q5SLB4)
-
brenda
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EXTERNAL LINKS (specific for EC-Number 7.6.2.10)
Transporter Classification Database (TCDB): 3.A.1.1.3
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Release 2023.1 (January 2023)
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