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Information on EC 7.5.2.1 - ABC-type maltose transporter
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EC Tree
7.5.2.1 ABC-type maltose 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. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides.
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Word Map
- 7.5.2.1
-
maltose-binding
- maltodextrins
-
outward-facing
-
proteoliposomes
- maltotriose
-
nanodiscs
-
atp-bound
-
inward-facing
-
atp-binding-cassette
-
lager
-
q-loops
- eiiaglc
- analysis
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
+
=
+
+
+
+
+
maltose-[maltose-binding protein][side 1]
=
+
+
+
[maltose-binding protein][side 1]
Synonyms
maltose transporter, malfgk2, mal11, malg511, malk2, maltose abc transporter, maltose atp-binding cassette transporter, maltose importer, malk3, maltose transporter malfgk2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP phosphohydrolase (maltose-importing)
-
-
-
-
Cg2463
EC 3.6.3.19
-
-
formerly
-
Mal11
MalFGK2
MalFGK2-E
the maltose transporter has 4 major domains: the heterodimeric transmembrane domains MalF and MalG, and the homodimeric nucleotide-binding domains MalK2
MalG511
-
the binding-protein-independent mutant L135F/I154S of Escherichia coli maltose transporter MalFGK2 retains specificity for maltose and shows a high basal ATPase activity in the absence of maltose binding protein
MalK
MalK2
MALT2
MALT4
maltose ABC transporter
maltose ATP-binding cassette importer
maltose ATP-binding cassette transporter
maltose transporter
maltose transporter ATPase
maltose-transporting ATPase
-
-
-
-
maltose/maltodextrin ABC transporter
MuSK
proton-maltose symporter
additional information
maltose ATP-binding cassette importer
-
-
maltose transporter
-
-
additional information
the enzyme belongs to the type I canonical ABC importers of the ATP-binding cassette, ABC, transporters
additional information
the maltose transporter is a member of the ATP-binding cassette, ABC, transporter superfamily
additional information
-
the enzyme belongs to the type I canonical ABC importers of the ATP-binding cassette, ABC, transporters
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + maltose-[maltose-binding protein][side 1] = ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, maltose-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. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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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 + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
P68187; P68183; P02916
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Saccharomyces eubayanus CBS 12357T
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Q9X0S9; Q9X2F5
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
Saccharomyces cerevisiae IMK289
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the putative helical domain of the nucleotide binding domains is involved, through its conformational changes, in the coupling between the transmembrane domains and the ATP binding/hydrolysis at the nucleotide-binding domains
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the peripheral membrane protein MalK associates with integral cytoplasmic membrane proteins MalF and MalG to form the maltose transport complex MalFGK. In addition malK participates in two different regulatory pathways which modulate mal gene expression and MalFGK transport activity
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
molecular dynamics simulations to study the ATP-driven association of the NBDs of the maltose ABC transporter, MalK, based on the crystal structures of its open and semiopen dimers, MgATP-dependent opening and closure, mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
extracytoplasmic anchoring of the substrate binding protein, the receptor, is emerging as key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle, molecular mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
maltose transport and ATPase activity of the MalFGK2 complex
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
structure and transport mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the transmembrane protein MalF, MalF-P2, of the maltose ATP-binding cassette transporter MalFGK2-E as an important element in the recognition of substrate by the maltose-binding protein MalE. MalF-P2 is not only responsible for substrate recognition, but also directly involved in activation of substrate transport. Substrate transport model for MalFGK2-E, isothermal titration calorimetry and molecular dynamics simulation, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
translocation of maltose across biological membranes
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
signal-transducing protein EIIAGlc interacts with the MalK subunits of the maltose ATP-binding cassette transporter
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP
-
-
?
additional information
?
-
-
interactions of MalK with the regulatory proteins MalT and enzyme IIAglc
-
-
?
additional information
?
-
-
concomitantly with the three conformations of the ATP-binding cassette MalK2, three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide-binding and periplasmic docking of liganded MalE to MalFG, overview
-
-
?
additional information
?
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
additional information
?
-
quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview
-
-
?
additional information
?
-
-
the periplasmic loop P2 of subunit MalF interacts with the maltose-binding potein MalE independently of the transmembrane region of MalF and MalG in the presence and absence of substrate, overview
-
-
?
additional information
?
-
the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity
-
-
?
additional information
?
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
additional information
?
-
-
although MalF and MalG differ in the number of transmembrane segments of 8 and 6, respectively, and their amino acid sequences, both contain the so-called EAA-motif, i.e. L-loop or coupling helix, which is in contact with MalK. MalF and MalG form a large central cavity for transport, but maltose is only bound to MalF. The MalK subunits bind and hydrolyze ATP, thereby generating the power stroke necessary for the rearrangements of MalFG, quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview
-
-
?
additional information
?
-
-
the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity
-
-
?
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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 + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
P68187; P68183; P02916
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Saccharomyces eubayanus CBS 12357T
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Q9X0S9; Q9X2F5
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
-
-
-
-
?
ATP + H2O + maltose-[maltose-binding protein][side 1] + H+[side1]
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] + H+[side2]
Saccharomyces cerevisiae IMK289
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
the peripheral membrane protein MalK associates with integral cytoplasmic membrane proteins MalF and MalG to form the maltose transport complex MalFGK. In addition malK participates in two different regulatory pathways which modulate mal gene expression and MalFGK transport activity
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
extracytoplasmic anchoring of the substrate binding protein, the receptor, is emerging as key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle, molecular mechanism, overview
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
-
-
-
?
ATP + H2O + maltose/out
ADP + phosphate + maltose/in
-
translocation of maltose across biological membranes
-
-
?
additional information
?
-
-
interactions of MalK with the regulatory proteins MalT and enzyme IIAglc
-
-
?
additional information
?
-
-
concomitantly with the three conformations of the ATP-binding cassette MalK2, three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide-binding and periplasmic docking of liganded MalE to MalFG, overview
-
-
?
additional information
?
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
additional information
?
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
stabilization of the semi-open MalK2 conformation by maltose-bound maltose-binding protein is key to the coupling of maltose transport to ATP hydrolysis in vivo, because it facilitates the progression of the MalK dimer from the open to the semi-open conformation, from which it can proceed to hydrolyze ATP
-
-
?
additional information
?
-
-
the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. the MalF P2 loop of the ATP-binding cassette transporter MalFGK2 interacts with maltose binding protein MalE throughout the catalytic cycle, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
structure of the nucleotide-binding domain of the maltose importer, comparison, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
required, bound to ATP, binding structure and mechanism of MgATP to the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antibody 4H12
-
recognizes the peptide 111-NQRVNQVAEVLQL-123
-
antibody 5B5
-
recognizes the peptide 53-ETITSGDLTRM-67
-
EIIAGlc
-
when glucose as preferred carbon source is transported, EIIAGlc becomes predominantly unphosphorylated and allosterically inhibits several permeases, including MalFGK2, which possesses a specific binding site in region III of EIIAGlc, in a process termed inducer exclusion involving the N-terminal part of the inhibitor, binding surface, overview
-
enzyme IIA(Glc)
-
inhibits the maltose ATP-binding cassette transporter MalE-FGK2 by interaction with the nucleotide-binding and -hydrolyzing subunit MalK
-
MalK
-
0.008 mM, in the absence of maltotriose 80% inhibition, no inhibition in the presence of 0.1 mM maltotriose
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MalF
-
MalF stimulates the substrate transport activity through its second periplasmic loop, overview
-
maltose binding protein
-
low levels of maltose binding protein stimulate enzyme activity
-
maltotetraose
5fold stimulation of ATPase activity at 0.6 mM
substrate-binding protein MalE
-
binds with high-affinity to MalFGK2 and facilitate the acquisition of maltose
-
verapamil
-
stimulates detergent-soluble maltose transporter, increases ATPase activity and lowers affinity for ATP
MalE
-
MalE and maltose together stimulate the ATPase activity of the enzyme. MalE stabilizes the enzyme in the outward-facing conformation
-
MalE
-
upon the binding of its periplasmic binding protein MalE, the ATPase activity of the enzyme can be greatly enhanced
-
maltose
-
MalE and maltose together stimulate the ATPase activity of the enzyme. Maltose triggers return to the inward-facing state for substrate and Pi release
maltose-binding protein
-
stimulates detergent-soluble maltose transporter, does not change the affinity of the complex for ATP but does increase the maximal rate of ATP hydrolysis
-
maltose-binding protein
-
required by wild-type strain, mutant strain does not require maltose-binding protein for transport. The major function of the maltose-binding protein is to send a transmembrane signal, in the presence of ligands, to the ATPase subunits on the inner side of the membrane. In addition it performs a special function in the translocation of the larger ligands, maltodextrins, perhaps by aligning them from entry into the channel
-
maltose-binding protein
-
a periplasmic maltose-binding protein, MBP, is required to stimulate the ATPase activity of the transporter. MBP stimulates ATP hydrolysis and initiates the transport process, it must interact with the resting state conformation to form a pretranslocation complex that is metastable in order to advance to the outward-facing conformation in the presence of ATP
-
maltose-binding protein
about 10dolf stimulation of activity at 0.005 mM
-
additional information
not stimulated by D-glucose, alpha-cyclodextrin, beta-cyclodextrin, and gamma-cyclodextrin
-
additional information
-
not stimulated by D-glucose, alpha-cyclodextrin, beta-cyclodextrin, and gamma-cyclodextrin
-
additional information
-
the ATPase activity of the maltose transporter MalFGK2 is dependent on interactions with the maltose-binding protein, MBP. A mutant sMBP, that can bind both maltose and sucrose, can stimulate ATPase activity of MalFGK2 to equal levels with either ligand bound, the activation is highly reduced compared to the wild-type MBP, structural basis and modeling the open sMBP structure bound to MalFGK2 in the transition state for ATP hydrolysis, mechanism and structure-function relationship, overview
-
additional information
the enzyme activity is independent of maltose
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Catabolite inactivation of the maltose transporter in nitrogen-starved yeast could be due to the stimulation of general protein turnover.
Starvation
Moderate concentrations of ethanol inhibit endocytosis of the yeast maltose transporter.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
maltose
-
Bacillus subtilis wild type, at 37°C, 0.001 mM 14C-labelled maltose (final concentration)
0.005
maltose
-
Bacillus subtilis strain MD195, mutant enzyme amyE, at 37°C, 0.001 mM 14C-labelled maltose (final concentration)
0.0075
maltose
-
Bacillus subtilis strain MD235, mutant enzyme mdxE, at 37°C, 0.001 mM 14C-labelled maltose (final concentration)
1.2
maltose-[maltose-binding protein][side 1]
-
mutant enzyme E167Q, at pH 5.5 and 30°C
-
4.5
maltose-[maltose-binding protein][side 1]
-
mutant enzyme E167A, at pH 5.5 and 30°C
-
4.6
maltose-[maltose-binding protein][side 1]
-
wild type enzyme, at pH 5.5 and 30°C
-
9.2
maltose-[maltose-binding protein][side 1]
-
mutant enzyme E120A, at pH 5.5 and 30°C
-
9.3
maltose-[maltose-binding protein][side 1]
-
mutant enzyme D123A, at pH 5.5 and 30°C
-
40.9
maltose-[maltose-binding protein][side 1]
-
mutant enzyme E120Q, at pH 5.5 and 30°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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avermectin production by wild-type and malEFG-a utant strains, overview
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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
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brenda
contains the maltose ABC transporter system encoded by malEFG-a
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brenda
contains the maltose ABC transporter system encoded by malEFG-a
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-
brenda
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brenda
subunits MalK, MalG, MalF, and MalE
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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the majority of the maltose binding protein is distributed throughout the cell wall, while only smaller quantities are located in the cytoplasmic membrane
brenda
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the majority of the maltose binding protein is distributed throughout the cell wall, while only smaller quantities are located in the cytoplasmic membrane
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brenda
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the maltose transport system consists of the periplasmic maltose-binding protein and the membrane proteins MalF, MalG, and MalK which form a heterotetrameric complex in the cytoplasmic membrane
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brenda
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the three membrane-associated components of the transport system MalF, MalG and MalK behave as a multiprotein complex
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brenda
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the proteins MalF and MalG are hydrophobic inner membrane components mediating the energy-dependent translocation of substrates into the cytoplasm, MalG spans the membrane six times and has its amino-terminus and its carboxy-terminus in the cytoplasm
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brenda
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the peripheral membrane protein MalK associates with integral cytoplasmic membrane proteins MalF and MalG to form the maltose transport complex MalFGK
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brenda
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the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit
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brenda
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extracytoplasmic anchoring of the substrate binding protein
brenda
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the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel is made up of MalF and MalG proteins, and two copies of the ATPase subunit
-
brenda
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the maltose transport system consists of the periplasmic maltose-binding protein and the membrane proteins MalF, MalG, and MalK which form a heterotetrameric complex in the cytoplasmic membrane
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
a series of spontaneous mutants of Lactococcus lactis IL1403 show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and also changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
malfunction
-
the addition of ATP and EDTA (to trigger the outwardfacing conformation) to the MBP-MalFGK2 system in the absence of maltose increases the mobility of W62C-SL in the MalG-DELTAscoop system but decreases it in the wild-type
malfunction
-
a series of spontaneous mutants of Lactococcus lactis IL1403 show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and also changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
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metabolism
the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen
metabolism
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the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen. The C-terminal domain of MalK has a dual regulatory function: it controls the activity of MalT, the positive transcriptional regulator of the maltose regulon, and it is the primary site at which dephosphorylated enzyme IIAGlc of the phosphoenolpyruvate phosphotransferase system binds, preventing maltose uptake
metabolism
-
the maltose ABC transporter is carbon catabolite repression-regulated
metabolism
-
the maltose transporter MalFGK2, together with the substrate-binding protein MalE, is a ABC transporter. MalE is bound in the periplasm with high-affinity to MalFGK2 to facilitate the acquisition of maltose. When the maltose concentration exceeds the transport capacity, MalE captures maltose and dissociates from the transporte, from the transporter past a threshold maltose concentration, in vivo, mechanism, overview. Maltose is both substrate and regulator of its own transporter, i.e. a homotropic regulator
metabolism
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the maltose ABC transporter is carbon catabolite repression-regulated
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physiological function
-
essential role of the maltose ABC transporter in the antimicrobial activity of garvicin ML
physiological function
-
the ATPase activity of the maltose transporter MalFGK2 is dependent on interactions with the maltose-binding protein, MBP
physiological function
-
the enzyme couples the energy from ATP hydrolysis to the active transport of substrates across the membrane
physiological function
-
the maltose ABC transporter MalFGK2 converts chemical energy from ATP hydrolysis to mechanical work for maltose substrate translocation. A periplasmic maltose-binding protein, MBP, is required to stimulate the ATPase activity of the transporter
physiological function
-
the enzyme genes MALT2 and MALT4 are essential for growth on maltose
physiological function
-
essential role of the maltose ABC transporter in the antimicrobial activity of garvicin ML
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physiological function
Saccharomyces eubayanus CBS 12357T
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the enzyme genes MALT2 and MALT4 are essential for growth on maltose
-
additional information
-
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
additional information
-
in the absence of MBP, MalFGK2 forms an inwardfacing conformation with the transmembrane-maltose-binding site exposed to the cytoplasm
additional information
-
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
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Show AA Sequence and Transmembrane Helices (2551 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
multimer
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the maltose transporter consists of a periplasmic maltose binding protein and a multisubunit membrane transporter, MalFGK2
additional information
?
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F,G,K2, the maltose transport system consists of the periplasmic maltose-binding protein and the membrane proteins MalF, MalG, and MalK which form a heterotetrameric complex in the cytoplasmic membrane
?
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the binding protein-dependent transport system for maltose and maltodextrins is composed of five proteins: LamB, MalE, MalF, MalG, and MalK
?
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F,G,K2, the three membrane-associated components of the transport system MalF, MalG and MalK behave as a multiprotein complex
?
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the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit
dimer
MalK structure comparison, the enzyme contains two cystathione beta-synthetase domains
additional information
the enzyme complex consists of two MalKs, MalF, MalG, and MBP, determination and analysis of the in-complex conformation of MalK. Walker A motif, the Q-loop, the LSGGQ motif, and the D-loop display low B-factors, dynamic behavior of the system, detailed overview
additional information
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the enzyme complex consists of two MalKs, MalF, MalG, and MBP, determination and analysis of the in-complex conformation of MalK. Walker A motif, the Q-loop, the LSGGQ motif, and the D-loop display low B-factors, dynamic behavior of the system, detailed overview
additional information
the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE
additional information
maltose transporter in the inward-facing conformation with rotation axes iand in outward-facing structure, overview
additional information
the maltose/maltodextrin transport system is composed of periplasmic maltose-binding protein, MalE, the pore-forming subunits MalF and MalG, and a homodimer of the nucleotide-binding subunit, MalK, overall structure, component interactions, and comparison, detailed overview. Structure modelling. The MalK dimer provides the energy for maltose transport by hydrolysing ATP. The structure of MalK is solved in two (nucleotide-free) apo-states, one ADP-bound and one ATP-bound state, representing two open, a semi-open and a closed conformation of the dimer, respectively, dynamics, overview
additional information
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the maltose transporter is an importer composed of two transmembrane subunits, MalF and MalG, and two subunits of a cytoplasmic adenosine triphosphatase (ATPase), MalK
additional information
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the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE
additional information
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the maltose/maltodextrin transport system is composed of periplasmic maltose-binding protein, MalE, the pore-forming subunits MalF and MalG, and a homodimer of the nucleotide-binding subunit, MalK, overall structure, component interactions, and comparison, detailed overview. Structure modelling.. The MalK dimer provides the energy for maltose transport by hydrolysing ATP
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MalE domain, sitting drop vapor diffusion method, using 100 mM BisTris, pH 5.5, 0.2 M LiSO4, 25% (w/v) PEG 3350
crystal structure analysis of full transporter MalFGK2 and of the MalF subunit
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crystal structure analysis, e.g. of the crystal structure of the complex in the presence of ATP and MalE, containing MalK mutant E159Q, is resolved at 2.8 A, revealing that MalFG are in a periplasmically open state
enzyme IIA in complex with the maltose transporter, vapor diffusion method, using 100 mM sodium cacodylate pH 5.6, 13% (w/v) PEG monomethylether 2000 and 100 mM NDSB-256
MalK crystal structure analysis in the semi-open, nucleotide-free, the open nucleotide-free, the ATP-bound, and the ADP-bound states
pre-translocation, outward- and inward-facing crystal structure analysis of enzyme complex with or without bound maltose binding protein and bound maltose and ATP, overview
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purified native MalFGK2 and and selenium methionine-labeled MalFGK2, in 20 mM Tris, pH 8.0, 50 mM NaCl, and 0.03% n-undecyl-beta-D-maltopyranoside, addtion of 5 mM 2-mercaptoethanol and 5 mM DTT for the SeMet-enzyme. Mixing of 1 mg/ml protein and reservoir solution, containing 11.5% PEG 4000, 0.1M N-(2-acetamido)iminodiacetic acid, pH 6.5, 0.1 M NaCl, and 0.1 M Li2SO4, in a 2:1 ratio, at 20°C in sitting drops, crystals appear after 24 h and grow to full size within 1 week, X-ray diffraction structure determination and anaylsis at 2.8 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C40S/S83C
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site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E
D380G
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substitution of aspartate for glycine in the maltose-binding site of MalF likely generates a futile cycle by preventing maltose from binding to MalFGK2 during the catalytic cycle
E159
the E159Q substitution in MalK prevents ATP from being hydrolysed. This results in an ATP-bound structure, which is thought to represent the transition state for ATP hydrolysis. The crystal shows an open (unliganded) MalE bound to the periplasmic side of the complex, a maltose molecule bound solely to a transmembrane region of MalF, and a closed conformation of the ATP-bound MalK(E59Q)2 subunits
E159Q
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the transporter containing the MalK-E159Q mutation is defective in ATP hydrolysis
L135F/I154S
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the binding-protein-independent mutant of Escherichia coli maltose transporter MalFGK2 retains specificity for maltose and shows a high basal ATPase activity in the absence of maltose binding protein
S205C/S252C
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site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E
T31C/S205C
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site-directed mutagensis, formation of a crosslink betwwen the mutant subunits
T31C/T177C
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site-directed mutagenesis, the distance between MalF mutant and MalE T31C mutant changes from 10 A to 5 A upon binding of ATP or maltose, with a less pronounced result, and is reset to 10 A after hydrolysis of one ATP
T80C/S205C
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site-directed mutagenesis, the mutation of subunit MalF mutant S205C does not affect the interaction with MalE mutant T80C
W230C
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site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
W340C
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site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
W62C
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site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retains good function in maltose transport and MBP-stimulated ATPase activities
Y155C
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site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein
Y341C
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site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retaines good function in maltose transport and MBP-stimulated ATPase activities
E120A
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the mutant shows strongly reduced activity compared to the wild type enzyme
E120A/D123A/E167A
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the mutations eliminate uphill maltose transport
E120N/D123N/E167N
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the mutations eliminate uphill maltose transport
E120Q
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the mutant shows reduced activity compared to the wild type enzyme
E120Q/D123Q/E167Q
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the mutations eliminate uphill maltose transport
E167A
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the mutant shows strongly reduced activity compared to the wild type enzyme
E167Q
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the mutant shows severely reduced activity compared to the wild type enzyme
E120A
Saccharomyces cerevisiae IMK289
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the mutant shows strongly reduced activity compared to the wild type enzyme
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E120Q
Saccharomyces cerevisiae IMK289
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the mutant shows reduced activity compared to the wild type enzyme
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E167A
Saccharomyces cerevisiae IMK289
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the mutant shows strongly reduced activity compared to the wild type enzyme
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E167Q
Saccharomyces cerevisiae IMK289
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the mutant shows severely reduced activity compared to the wild type enzyme
-
T31C/S205C
-
site-directed mutagensis, formation of a crosslink betwwen the mutant subunits
T31C/T177C
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site-directed mutagenesis, the distance between MalF mutant and MalE T31C mutant changes from 10 A to 5 A upon binding of ATP or maltose, with a less pronounced result, and is reset to 10 A after hydrolysis of one ATP
T80C/S205C
-
site-directed mutagenesis, the mutation of subunit MalF mutant S205C does not affect the interaction with MalE mutant T80C
G137A
-
mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
G137T
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mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
G137V
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mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, loss of ability to hydrolyze ATP, but still displays nucleotide-binding activity
Q140K
Q140L
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mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, fails to hydrolyze ATP and exhibits a strong intrinsic resistance to trypsin in the absence of MgATP, suggesting a drastically altered conformation
Q140N
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mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140N variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity
additional information
Q140K
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mutation in MalK, fails to restore a functional transport complex in vivo, mutation increases the repressing activity of MalK on other maltose-regulated genes, ATPase activity and MgATP-induced changes in tryptic cleavage pattern similar to those of wild-type. Mutant transport complexes containing MalKQ140K variant, when studied in proteoliposomes, are severely impaired in MalE-maltose-stimulated ATPase activity
Q140K
-
normal intrinsic ATPase activity in soluble state but no hydrolysis of ATP when assembled with MalFG
additional information
-
construction of a fusion protein of MalE and the hydrophobic membrane protein MalG
additional information
-
insertion mutants: the insertion introduce 31 mostly hydrophilic amino acids into the protein. MalK mutants with insertion after residues 275, 291, 346 and 364, apparently have lost the ability to participate in MalT-dependent mal gene regulation
additional information
-
cystein-free enzyme shows no change in activity compared to wild-type enzyme
additional information
-
the MalK2 ATP hydrolysis cycle does not induce MalF-P2 loop rearrangements in the absence of MalE
additional information
-
in deletion mutant MalG-DELTAscoop a four-residue deletion of a periplasmic loop of MalG limits its reach into the maltose-binding pocket of MBP, allowing maltose to remain associated with MBP during the catalytic cycle. Uncoupling of transport and ATP hydrolysis in the MalG-DELTAscoop and MalF-G380D mutants, overview
additional information
-
generation of a series of spontaneous mutants of Lactococcus lactis IL1403 with a large deletion in a chromosomal region involved in carbohydrate metabolism. The mutants show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
additional information
-
generation of a series of spontaneous mutants of Lactococcus lactis IL1403 with a large deletion in a chromosomal region involved in carbohydrate metabolism. The mutants show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin
-
additional information
-
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
additional information
-
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
maltose-binding protein effectively stabilizes the partially closed conformation of the enzyme
-
MgATP2-, binding protects against trypsin inactivation in wild-type enzyme in in G137 mutants
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cobalt resin column chromatography and Talon resin column chromatography
cobalt-affinity column chromatography and Superdex 200 gel filtration
purification of recombinant subunits
-
recombinant His-tagged enzyme from Escherichia coli strain JM109
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain JM109 by nickel affinity chromatography and ultrafiltration
recombinant wild-type and mutant MalFGK2 from Escherichia coli strain AD110 by cobalt affinity chromatography and gel filtration
Talon-HiTrap resin column chromatography, and Superdex 200 gel filtration
wild-type strain and mutant strain that does not require maltose-binding protein for transport
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recombinant His-tagged enzyme from Escherichia coli strain JM109
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain JM109 by nickel affinity chromatography and ultrafiltration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain JM109 by nickel affinity chromatography and ultrafiltration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a maltose-transport-deficient Saccharomyces cerevisiae strain IMZ616
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expression in Escherichia coli
genes malEFG-a, encoding the maltose ABC transporter system, transcriptional analysis of malE-a by RT-PCR, and malEFG-a gene replacement cloning
-
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
recombinant His-tagged enzyme expression in Escherichia coli strain JM109
the type I maltose ABC importer is encoded within the maltose regulon
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
-
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain JM109
-
recombinant His-tagged enzyme expression in Escherichia coli strain JM109
-
recombinant His-tagged enzyme expression in Escherichia coli strain JM109
the type I maltose ABC importer is encoded within the maltose regulon
-
the type I maltose ABC importer is encoded within the maltose regulon
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of malE-a is induced by maltose
expression of malE-a is strongly repressed by glucose
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant purified MalFGK2 are reconstituted into proteoliposomes at a lipid-to-protein ratio of 100:1 in g/ml
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis
analysis
-
the maltose/maltodextrin transport system of Escherichia coli/Salmonella serves as a model for canonical ATP-binding cassette importers in general
analysis
the maltose/maltodextrin transport system of Escherichia coli/Salmonella serves as a model for canonical ATP-binding cassette importers in general
synthesis
-
overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production, which is useful for the improvement of commercial antibiotic production using starch as the main carbon source in the fermentation process
synthesis
-
overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production, which is useful for the improvement of commercial antibiotic production using starch as the main carbon source in the fermentation process
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dassa, E.; Lambert, P.
Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein
Res. Microbiol.
148
389-395
1997
Escherichia coli
brenda
Panagiotidis, C.H.; Reyes, M.; Sievertsen, A.; Boos, W.; Shuman, H.A.
Characterization of the structural requirements for assembly and nucleotide binding cassette transporter. The maltose transport system of Escherichia coli
J. Biol. Chem.
268
23685-23696
1993
Escherichia coli
brenda
Davidson, A.L.; Nikaido, H.
Purification and characterization of the membrane associated components of the maltose transport system from Escherichia coli
J. Biol. Chem.
266
8946-8951
1991
Escherichia coli
brenda
Mourez, M.; Jehanno, M.; Schneider, E.; Dassa, E.
In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP
Mol. Microbiol.
30
353-363
1998
Escherichia coli
brenda
Dassa, E.; Muir, S.
Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli
Mol. Microbiol.
7
29-38
1993
Escherichia coli
brenda
Nikaido, H.
Maltose transport system of Escherichia coli: an ABC-type transporter
FEBS Lett.
346
55-58
1994
Escherichia coli
brenda
Hulsmann, A.; Lurz, R.; Scheffel, F.; Schneider, E.
Maltose and maltodextrin transport in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius is mediated by a high-affinity transport system that includes a maltose binding protein tolerant to low pH
J. Bacteriol.
182
6292-6301
2000
Alicyclobacillus acidocaldarius
brenda
Reich-Slotky, R.; Panagiotidis, C.; Reyes, M.; Shuman, H.A.
The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
J. Bacteriol.
182
993-1000
2000
Escherichia coli
brenda
Lippincott, J.; Traxler, B.
MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants
J. Bacteriol.
179
13337-1343
1997
Escherichia coli
brenda
Nelson, B.D.; Traxler, B.
Exploring the role of integral membrane proteins in ATP-binding cassette transporters: analysis of a collection of MalG inserion mutants
J. Bacteriol.
180
2507-2514
1998
Escherichia coli
brenda
Schmees, G.; Stein, A.; Hunke, S.; Landmesser, H.; Schneider, E.
Functional consequences of mutation in the conserved signature sequence of the ATP-binding-cassette protein MalK
Eur. J. Biochem.
266
420-430
1999
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Landmesser, H.; Stein, A.; Bluschke, B.; Brinkmann, M.; Hunke, S.; Schneider, E.
Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK2) of Salmonella typhimurium
Biochim. Biophys. Acta
1565
64-72
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Scheffel, F.; Fleischer, R.; Schneider, E.
Functional reconstitution of a maltose ATP-binding cassette transporter from the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius
Biochim. Biophys. Acta
1656
57-65
2004
Alicyclobacillus acidocaldarius (Q70HW1), Alicyclobacillus acidocaldarius
brenda
Greller, G.; Riek, R.; Boos, W.
Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis
Eur. J. Biochem.
268
4011-4018
2001
Thermococcus litoralis
brenda
Stein, A.; Seifert, M.; Volkmer-Engert, R.; Siepelmeyer, J.; Jahreis, K.; Schneider, E.
Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit
Eur. J. Biochem.
269
4074-4085
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Samanta, S.; Ayvaz, T.; Reyes, M.; Shuman, H.A.; Chen, J.; Davidson, A.L.
Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two malK subunits in the maltose transport complex
J. Biol. Chem.
278
35265-35271
2003
Escherichia coli
brenda
Austermuhle, M.I.; Hall, J.A.; Klug, C.S.; Davidson, A.L.
Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport
J. Biol. Chem.
279
28243-28250
2004
Escherichia coli
brenda
Schoenert, S.; Seitz, S.; Krafft, H.; Feuerbaum, E.; Andernach, I.; Witz, G.; Dahl, M.K.
Maltose and maltodextrin utilization by Bacillus subtilis
J. Bacteriol.
188
3911-3922
2006
Bacillus subtilis
brenda
Joly, N.; Boehm, A.; Boos, W.; Richet, E.
MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding
J. Biol. Chem.
279
33123-33130
2004
Escherichia coli
brenda
Horn, C.; Jenewein, S.; Tschapek, B.; Bouschen, W.; Metzger, S.; Bremer, E.; Schmitt, L.
Monitoring conformational changes during the catalytic cycle of OpuAA, the ATPase subunit of the ABC transporter OpuA from Bacillus subtilis
Biochem. J.
412
233-244
2008
Escherichia coli (P68187), Escherichia coli
brenda
Blueschke, B.; Volkmer-Engert, R.; Schneider, E.
Topography of the surface of the signal-transducing protein EIIAGlc that interacts with the MalK subunits of the maltose ATP-binding cassette transporter (MalFGK2) of Salmonella typhimurium
J. Biol. Chem.
281
12833-12840
2006
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Oloo, E.O.; Fung, E.Y.; Tieleman, D.P.
The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter
J. Biol. Chem.
281
28397-28407
2006
Escherichia coli
brenda
Jacso, T.; Grote, M.; Daus, M.; Schmieder, P.; Keller, S.; Schneider, E.; Reif, B.
The periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE
Biochemistry
48
2216-2225
2009
Escherichia coli
brenda
Grote, M.; Bordignon, E.; Polyhach, Y.; Jeschke, G.; Steinhoff, H.J.; Schneider, E.
A comparative electron paramagnetic resonance study of the nucleotide-binding domains catalytic cycle in the assembled maltose ATP-binding cassette importer
Biophys. J.
95
2924-2938
2008
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P68187)
brenda
Daus, M.L.; Grote, M.; Schneider, E.
The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle
J. Bacteriol.
191
754-761
2009
Escherichia coli, Salmonella enterica
brenda
Grote, M.; Polyhach, Y.; Jeschke, G.; Steinhoff, H.J.; Schneider, E.; Bordignon, E.
Transmembrane signaling in the maltose ABC transporter MALFGK2-E: The periplasmic MALF-P2 loop communicates substrate availability to the ATP-bound malk dimer
J. Biol. Chem.
284
17521-17526
2009
Escherichia coli
brenda
Lukman, S.; Grant, G.H.
A network of dynamically conserved residues deciphers the motions of maltose transporter
Proteins
76
588-597
2009
Escherichia coli (P68187), Escherichia coli
brenda
Li, M.; Chen, Z.; Zhang, X.; Song, Y.; Wen, Y.; Li, J.
Enhancement of avermectin and ivermectin production by overexpression of the maltose ATP-binding cassette transporter in Streptomyces avermitilis
Biores. Technol.
101
9228-9235
2010
Streptomyces avermitilis, Streptomyces avermitilis ATCC 31267
brenda
Khare, D.; Oldham, M.L.; Orelle, C.; Davidson, A.L.; Chen, J.
Alternating access in maltose transporter mediated by rigid-body rotations
Mol. Cell
33
528-536
2009
Escherichia coli (P68187)
brenda
Bordignon, E.; Grote, M.; Schneider, E.
The maltose ABC transporter in the 21(st) century - towards a structural-dynamic perspective on its mode of action
Mol. Microbiol.
77
1354-1366
2010
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P68187)
brenda
Gabrielsen, C.; Brede, D.; Hernandez, P.; Nes, I.; Diep, D.
The maltose ABC transporter in Lactococcus lactis facilitates high-level sensitivity to the circular bacteriocin garvicin ML
Antimicrob. Agents Chemother.
56
2908-2915
2012
Lactococcus lactis, Lactococcus lactis IL1403
brenda
Gould, A.; Shilton, B.
Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate
J. Biol. Chem.
285
11290-11296
2010
Escherichia coli
brenda
Cui, J.; Qasim, S.; Davidson, A.
Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter
J. Biol. Chem.
285
39986-39993
2010
Escherichia coli
brenda
Jacso, T.; Schneider, E.; Rupp, B.; Reif, B.
Substrate transport activation is mediated through second periplasmic loop of transmembrane protein MalF in maltose transport complex of Escherichia coli
J. Biol. Chem.
287
17040-17049
2012
Escherichia coli
brenda
Bao, H.; Duong, F.
Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2
PLoS ONE
7
e34836
2012
Escherichia coli
brenda
Oldham, M.; Chen, J.
Crystal structure of the maltose transporter in a pretranslocation intermediate state
Science
332
1202-1205
2011
Escherichia coli
brenda
Bao, H.; Dalal, K.; Wang, V.; Rouiller, I.; Duong, F.
The maltose ABC transporter: action of membrane lipids on the transporter stability, coupling and ATPase activity
Biochim. Biophys. Acta
1828
1723-1730
2013
Escherichia coli
brenda
Henrich, A.; Kuhlmann, N.; Eck, A.W.; Kraemer, R.; Seibold, G.M.
Maltose uptake by the novel ABC transport system MusEFGK2I causes increased expression of ptsG in Corynebacterium glutamicum
J. Bacteriol.
195
2573-2584
2013
Corynebacterium glutamicum (Q8NMV1), Corynebacterium glutamicum ATCC 13032 (Q8NMV1)
brenda
Alvarez, F.J.; Orelle, C.; Huang, Y.; Bajaj, R.; Everly, R.M.; Klug, C.S.; Davidson, A.L.
Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter
Mol. Microbiol.
98
878-894
2015
Escherichia coli (P68187), Escherichia coli
brenda
Chen, S.; Oldham, M.L.; Davidson, A.L.; Chen, J.
Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography
Nature
499
364-368
2013
Escherichia coli (P68187), Escherichia coli
brenda
Boehm, S.; Licht, A.; Wuttge, S.; Schneider, E.; Bordignon, E.
Conformational plasticity of the type I maltose ABC importer
Proc. Natl. Acad. Sci. USA
110
5492-5497
2013
Escherichia coli (P68187), Escherichia coli
brenda
Singh, R.; White, D.; Blum, P.
Identification of the ATPase subunit of the primary maltose transporter in the hyperthermophilic anaerobe Thermotoga maritima
Appl. Environ. Microbiol.
83
pii: e00930-17
2017
Thermotoga maritima (Q9X0S9 AND Q9X2F5), Thermotoga maritima
brenda
Wuttge, S.; Licht, A.; Timachi, M.H.; Bordignon, E.; Schneider, E.
Mode of interaction of the signal-transducing protein EIIA(Glc) with the maltose ABC transporter in the process of inducer exclusion
Biochemistry
55
5442-5452
2016
Escherichia coli
brenda
Bajaj, R.; Park, M.I.; Stauffacher, C.V.; Davidson, A.L.
Conformational dynamics in the binding-protein-independent mutant of the Escherichia coli maltose transporter, MalG511, and its interaction with maltose binding protein
Biochemistry
57
3003-3015
2018
Escherichia coli
brenda
Brickwedde, A.; Brouwers, N.; van den Broek, M.; Gallego Murillo, J.S.; Fraiture, J.L.; Pronk, J.T.; Daran, J.G.
Structural, physiological and regulatory analysis of maltose transporter genes in Saccharomyces eubayanus CBS 12357T
Front. Microbiol.
9
1786
2018
Saccharomyces eubayanus, Saccharomyces eubayanus CBS 12357T
brenda
Bao, H.; Dalal, K.; Cytrynbaum, E.; Duong, F.
Sequential action of MalE and maltose allows coupling ATP hydrolysis to translocation in the MalFGK2 transporter
J. Biol. Chem.
290
25452-25460
2015
Escherichia coli
brenda
Carlson, M.L.; Bao, H.; Duong, F.
Formation of a chloride-conducting state in the maltose ATP-binding cassette (ABC) transporter
J. Biol. Chem.
291
12119-12125
2016
Escherichia coli (P68187 and P68183 and P02916)
brenda
Hsu, W.L.; Furuta, T.; Sakurai, M.
Analysis of the free energy landscapes for the opening-closing dynamics of the maltose transporter ATPase MalK2 using enhanced-sampling molecular dynamics simulation
J. Phys. Chem. B
119
9717-9725
2015
Escherichia coli
brenda
Hsu, W.L.; Furuta, T.; Sakurai, M.
ATP hydrolysis mechanism in a maltose transporter explored by QM/MM metadynamics simulation
J. Phys. Chem. B
120
11102-11112
2016
Escherichia coli
brenda
Weng, J.; Gu, S.; Gao, X.; Huang, X.; Wang, W.
Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2
Phys. Chem. Chem. Phys.
19
9366-9373
2017
Escherichia coli
brenda
Lv, X.; Liu, H.; Chen, H.; Gong, H.
Coupling between ATP hydrolysis and protein conformational change in maltose transporter
Proteins
85
207-220
2017
Escherichia coli (P68187)
brenda
Hsu, W.L.; Furuta, T.; Sakurai, M.
The mechanism of nucleotide-binding domain dimerization in the intact maltose transporter as studied by all-atom molecular dynamics simulations
Proteins
86
237-247
2018
Escherichia coli (P68187 and P68183 and P02916 and P0AEX9), Escherichia coli
brenda
Licht, A.; Bommer, M.; Werther, T.; Neumann, K.; Hobe, C.; Schneider, E.
Structural and functional characterization of a maltose/maltodextrin ABC transporter comprising a single solute binding domain (MalE) fused to the transmembrane subunit MalF
Res. Microbiol.
170
1-12
2019
Bdellovibrio bacteriovorus (Q6MNM0), Bdellovibrio bacteriovorus, Bdellovibrio bacteriovorus HD100 (Q6MNM0)
brenda
Henderson, R.; Poolman, B.
Proton-solute coupling mechanism of the maltose transporter from Saccharomyces cerevisiae
Sci. Rep.
7
14375
2017
Saccharomyces cerevisiae, Saccharomyces cerevisiae IMK289
brenda
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EXTERNAL LINKS (specific for EC-Number 7.5.2.1)
Transporter Classification Database (TCDB): 3.A.1.1.1
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Release 2023.1 (January 2023)
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