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Information on EC 7.6.2.9 - ABC-type quaternary amine transporter
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EC Tree
7.6.2.9 ABC-type quaternary amine 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 quaternary amine derivatives.
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Word Map
- 7.6.2.9
- cassette
-
multidrug
- p-glycoprotein
-
nucleotide-binding
- toxin
- streptococcus
- lipoprotein
- xenobiotics
-
bacteriocins
- azole
- doxorubicin
- verapamil
-
siderophore
- cftr
-
resistance-associated
-
chemoresistance
- lactococcus
-
two-component
-
hoechst
-
cystic
- rhodamine
- elasticum
-
atp-bound
- nisin
- mitoxantrone
- molecular biology
-
cry1ac
-
abc-transporter
-
abcb11
-
azole-resistant
-
calcein
- ivermectin
-
proteoliposomes
-
atp-driven
-
lantibiotic
-
abcg2-mediated
-
pseudoxanthoma
- flippase
-
abccs
-
transporter-mediated
- thuringiensis
-
triphosphate-binding
-
outward-facing
-
canalicular
- stargardt
- bacitracin
- adrenoleukodystrophy
- fluconazole
-
nucleotide-free
- itraconazole
-
inward-facing
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
+
+
+
+
quaternary amine-[quaternary amine-binding protein][side 1]
=
+
+
quaternary amine[side 2]
+
[quaternary amine-binding protein][side 1]
Synonyms
abc transporter, opuac, glycine betaine-binding protein, opubc, opucc, glycine betaine porter ii, opuab, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.6.3.32
-
-
formerly
-
glycine betaine transport system permease protein
glycine betaine transporter membrane protein
glycine betaine-binding protein
glycine betaine-binding protein OpuAC
glycine/betaine ABC transporter
N288_21505
N288_21525
N288_25665
OpuA
OpuAB
OpuAC
OpuB
OpuBC
OpuC
OpuF
OpuF transporter
proline/betaine ABC transporter permease
proW
Quaternary-amine-transporting ATPase
-
-
-
-
glycine betaine transporter membrane protein
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
UniProt
glycine betaine transporter membrane protein
Vibrio anguillarum serotype O1 MVM425
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
UniProt
-
OpuB
-
opuB and opuC operons each encode a binding protein-dependent ABC transport system
OpuC
-
opuB and opuC operons each encode a binding protein-dependent ABC transport system
proline/betaine ABC transporter permease
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
UniProt
proline/betaine ABC transporter permease
Vibrio anguillarum serotype O1 MVM425
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
UniProt
-
proW
Vibrio anguillarum serotype O1 MVM425
A0A077T980; A0A077T7U5; A0A077T7Z1
-
-
proW
Vibrio anguillarum serotype O1 MVM425
A0A077T980; A0A077T7U5; A0A077T7Z1
UniProt
-
proW
Vibrio anguillarum serotype O1 MVM425
A0A097A5F2; A0A077T7R8
-
-
proW
Vibrio anguillarum serotype O1 MVM425
A0A097A5F2; A0A077T7R8
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
a single substrate binding domain per dimeric translocator complex is sufficient and minimally needed for transport. Within the complex with two substrate binding domains, the two domains interact in a cooperative manner and enhance the transport capacity
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
busA locus encodes the glycine betaine uptake system, which expression is reduced by overexpression of busR gene encoding a DNA binding protein
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
OpuA is an osmoprotectant uptake system which imports glycine and betaine. It consists of three components, the ATPase OpuAA, the integral membrane protein OpuAB and the extracellular substrate binding domain OpuAC. The ABC transporter couples ATP hydrolysis with substrate translocation across the membrane in a vectorial manner
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
the mechanistica stoichiometry is 2
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
the osmotic activation of the transporter is set by the bulk charge in the lipid headgroup region of the membrane, indicating that electrostatic interactions between lipids and the transporter are intrinsic to the osmosensing mechanism
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
a single substrate binding domain per dimeric translocator complex is sufficient and minimally needed for transport. Within the complex with two substrate binding domains, the two domains interact in a cooperative manner and enhance the transport capacity
-
-
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
the mechanistica stoichiometry is 2
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, quaternary-amine-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 quaternary amine derivatives.
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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
AMP + H2O
adenine + phosphate
-
OpuAA protein, ATPase activity, similar substrate affinities to monomeric and dimeric states
-
-
?
ATP + H2O + L-proline betaine/out
ADP + phosphate + L-proline betaine/in
-
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
ATP + H2O
ADP + phosphate
ATPase activity of monomeric OpuA protein measured in wild-type and single cysteine mutants, structural information on the architecture of the OpuA-ATPase by application of FRET techniques, C-terminal catalytic domain, helical domain and accessory domain analyzed
-
-
?
ATP + H2O + dimethylsulfonioacetate/out
ADP + phosphate + dimethylsulfonioacetate/in
OpuA is a classic ABC importer that relies on a substrate binding protein priming the transporter with specificity and selectivity
-
-
?
ATP + H2O + dimethylsulfonioacetate/out
ADP + phosphate + dimethylsulfonioacetate/in
a sulfobetaine
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
high osmolarity stimulates de novo synthesis of OpuD and activates preeixisting OpuD proteins to achieve maximal glycine betaine uptake activity
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
expression of the opuA operon is under osmotic control
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
expression of the opuA operon is under osmotic control
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
accumulation of glycine betaine which functions as an osmoprotectant, the glycine betaine transport system is osmotically regulated at the level of gene expression and at the level of transport activity
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
glycine betaine binds to the substrate-binding protein component ProX of ProU with high-affinity and is then transported via nucleotide-binding and transmembrane proteins ProXVW in an ATP-dependent manner
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
OpuAC is highly specific for glycine betaine and the related proline betaine
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
a transmembrane osmotic gradient, outside hyperosmotic relative to the inside, of both ionic and nonionic compounds is able to osmotically activate OpuA. OpuA can act both as osmosensor and osmoregulator
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
enzyme is involved in cytoplasmic accumulation of exogenous betaine which has osmoprotective properties, transcription of busA is strongly regulated by the external osmolarity of the medium
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
no efflux of glycine betaine is observed in the absence of ATP
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
no efflux of glycine betaine is observed in the absence of ATP
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
a transmembrane osmotic gradient, outside hyperosmotic relative to the inside, of both ionic and nonionic compounds is able to osmotically activate OpuA. OpuA can act both as osmosensor and osmoregulator
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
enzyme is involved in cytoplasmic accumulation of exogenous betaine which has osmoprotective properties, transcription of busA is strongly regulated by the external osmolarity of the medium
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
enzyme is responsible for the cold-activated and osmotically activated glycine betaine transport
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
the ability of the food-borne pathogen Listeria monocytogenes to tolerate environments of elevated osmolarity and reduced temperature is due in part to the transport and accumulation of the osmolyte glycine betaine by the glycine betaine transport system
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
effects of glycine betaine on the survival of Listeria monocytogenes on leaf surfaces under low humidity studied, protective effect of glycine betaine on survival determined, independence of intracellular glycine betaine accumulation by known uptake systems shown
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
effects of glycine betaine on the survival of Listeria monocytogenes on leaf surfaces under low humidity studied, protective effect of glycine betaine on survival determined, independence of intracellular glycine betaine accumulation by known uptake systems shown
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
enhanced osmoprotection found to be correlated with higher capacity for choline uptake than for glycine uptake, broad substrate specificity including acetylcholine, carnitine, and proline betaine determined, cystathionine-beta-synthase domains shown to be essential for osmoregulatory function
-
-
?
ATP + H2O + proline betaine/out
ADP + phosphate + proline betaine/in
-
-
-
-
?
ATP + H2O + proline betaine/out
ADP + phosphate + proline betaine/in
-
OpuAC is highly specific for glycine betaine and the related proline betaine
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
U5LFB4; U5LHK3; U5LHN4
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
U5LFB4; U5LHK3; U5LHN4
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
Vibrio anguillarum serotype O1 MVM425
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
-
-
-
?
ATP + H2O + quaternary amine/out
ADP + phosphate + quaternary amine/in
-
-
-
-
?
ATP + H2O + quaternary amine/out
ADP + phosphate + quaternary amine/in
-
-
-
-
?
additional information
?
-
analysis of the OpuA-binding protein OpuAC by structural and mutational means with respect to dimethylsulfonioacetate binding, crystal structure determination and analysis, overview
-
-
?
additional information
?
-
-
analysis of the OpuA-binding protein OpuAC by structural and mutational means with respect to dimethylsulfonioacetate binding, crystal structure determination and analysis, overview
-
-
?
additional information
?
-
-
carnitine is no substrate for the enzyme
-
-
?
additional information
?
-
other solute like proline and carnitine bind with affinities that are 3 to 4 orders of magnitude lower than for glycine betaine or proline betaine
-
-
?
additional information
?
-
-
other solute like proline and carnitine bind with affinities that are 3 to 4 orders of magnitude lower than for glycine betaine or proline betaine
-
-
?
additional information
?
-
-
carnitine is no substrate for the enzyme
-
-
?
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 + dimethylsulfonioacetate/out
ADP + phosphate + dimethylsulfonioacetate/in
OpuA is a classic ABC importer that relies on a substrate binding protein priming the transporter with specificity and selectivity
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
high osmolarity stimulates de novo synthesis of OpuD and activates preeixisting OpuD proteins to achieve maximal glycine betaine uptake activity
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
expression of the opuA operon is under osmotic control
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
expression of the opuA operon is under osmotic control
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
accumulation of glycine betaine which functions as an osmoprotectant, the glycine betaine transport system is osmotically regulated at the level of gene expression and at the level of transport activity
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
a transmembrane osmotic gradient, outside hyperosmotic relative to the inside, of both ionic and nonionic compounds is able to osmotically activate OpuA. OpuA can act both as osmosensor and osmoregulator
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
enzyme is involved in cytoplasmic accumulation of exogenous betaine which has osmoprotective properties, transcription of busA is strongly regulated by the external osmolarity of the medium
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
a transmembrane osmotic gradient, outside hyperosmotic relative to the inside, of both ionic and nonionic compounds is able to osmotically activate OpuA. OpuA can act both as osmosensor and osmoregulator
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
enzyme is involved in cytoplasmic accumulation of exogenous betaine which has osmoprotective properties, transcription of busA is strongly regulated by the external osmolarity of the medium
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
enzyme is responsible for the cold-activated and osmotically activated glycine betaine transport
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
the ability of the food-borne pathogen Listeria monocytogenes to tolerate environments of elevated osmolarity and reduced temperature is due in part to the transport and accumulation of the osmolyte glycine betaine by the glycine betaine transport system
-
-
?
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
-
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
U5LFB4; U5LHK3; U5LHN4
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
U5LFB4; U5LHK3; U5LHN4
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
-
-
-
?
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1]
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
Vibrio anguillarum serotype O1 MVM425
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
-
-
-
?
ATP + H2O + quaternary amine/out
ADP + phosphate + quaternary amine/in
-
-
-
-
?
ATP + H2O + quaternary amine/out
ADP + phosphate + quaternary amine/in
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
bivalent cations more effective activators than monovalent cations
K+
K3PO4
-
100 mosmol/kg osmolality, pH 7.0, stimulates OpuA activity. 200 mM, stimulates ATPase activity
Mg2+
Na+
NH4+
less effective than KCl, in the presence of the protonophore SF6847 much more effective
Sodium phosphate
-
100 mosmol/kg osmolality, pH 7.0, stimulates OpuA activity
additional information
K+
-
K+ binding site within the nucleotide-binding protein domain, stimulation of the nucleotide-binding protein domain 4fold higher than with Na+
K+
maximal enzyme activity reached with 250 mM KCl, no further effect in the presence of the protonophore SF6847
Mg2+
-
significant reduction of glycine betaine efflux when 6 mM ADP/Mg2+ is added to the reaction
Mg2+
bivalent cations more effective activators than monovalent cations
Mg2+
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
required
Na+
-
stimulation of the nucleotide-binding protein domain 4fold lower than with K+
Na+
-
osmotically activated but does not require high concentrations for activity
additional information
K+, Li+, Cs+, Rb+, NH4+, Ca2+, and Mg2+ show no effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tetracaine
-
low concentrations of the cationic amphipath decrease the activation of OpuA
additional information
betaine uptake not inhibited by gamma-aminobutyric acid, proline, glutamate, aspartate, glutamine, asparagine, glycine, sarcosine, dimethylglycine, lysine, histidine, alanine, leucine, isoleucine, serine, cysteine, threonine, valine, phenylalanine, tryptophan, and methionine
-
additional information
-
the enzyme is not inhibited by 400 mM glycine betaine on the trans side of the membrane. The enzyme is not inhibited by 250 mM carnitine
-
additional information
competition assays performed, compounds inhibiting the uptake of choline and glycine betaine summarized
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
anionic lipids
-
absence of phosphatidylglycerol and/or phosphatidylserine results in trapping of the protein in an inactive state
-
dioleoyl-phosphatidylglycerol
needed for full osmoregulatory activity
glycerol
-
at 270 mM, the amount of glycine betaine taken up after 30 seconds is 30% higher than that of the iso-osmotic control sample
phosphatidylethanolamine
-
non-bilayer lipid essential for high activity of OpuA
Tetracaine
instantaneously activates inside-out oriented OpuA, reconstitued in membranes with 40% of anionic lipid, 1mM equally effective than 0.2 mM KCl
additional information
-
nucleotide-binding protein domain not stimulated by glycine betaine
-
additional information
-
sucrose and D-fructose have no effects on OpuA activity
-
additional information
the binding of glycine betaine to purified OpuA and OpuAC does not show any salt dependence or cooperative effects, in contrast to the transport activity
-
additional information
-
the binding of glycine betaine to purified OpuA and OpuAC does not show any salt dependence or cooperative effects, in contrast to the transport activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
ATP
wild-type, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form
0.7
ATP
mutant S45C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form
1.7
ATP
mutant F19W, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form
2.8
ATP
mutant G161C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form
0.00832
betaine
Aphanothece halophytica cells supplemented with 0.5 M NaCl
0.00941
betaine
Aphanothece halophytica cells supplemented with 2.0 M NaCl
0.0919
betaine
at pH 8.5, BetTA.halophytica expressing MKH13 cells
0.128
betaine
at pH 7.0, BetTA.halophytica expressing MKH13 cells
0.272
betaine
at pH 5.5, BetTA.halophytica expressing MKH13 cells
0.0019
glycine betaine
-
30ºC, pH 7.0, wild type/substrate binding domain-less mutant heterodimer
0.0037
glycine betaine
kinetics of OpuC-mediated uptake, in 50 mM of phosphate buffer containing 0.5 M of NaCl, 0.2% glucose, pH 7, low-affinity transport of choline determined
additional information
additional information
U5LFB4; U5LHK3; U5LHN4
dissociation constants of recombinant OpuAR for choline and glycine betaine are determined by intrinsic tryptophan fluorescence spectroscopy
-
additional information
additional information
kinetic parameters for the uptake of glycine betaine via the hybrid ABC transporter OpuB::OpuCC expressed in the parent engineered strain LTB1 and its three suppressor derivatives
-
additional information
additional information
kinetic parameters for the uptake of glycine betaine via the hybrid ABC transporter OpuB::OpuCC expressed in the parent engineered strain LTB1 and its three suppressor derivatives
-
additional information
additional information
-
kinetic parameters for the uptake of glycine betaine via the hybrid ABC transporter OpuB::OpuCC expressed in the parent engineered strain LTB1 and its three suppressor derivatives
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.009
-
ATPase activity, pH 7.0, 50 mM K3PO4, 290 mM sucrose, 450 mosmol/kg
additional information
additional information
studies on architecture and potential roles of the C-terminal accessory domain in structural and functional protein regulation performed, conformational changes during the catalytic cycle of the ATPase unit of OpuA protein determined, single cysteine mutants generated, static and time-resolved FRET measurements applied, molecular modelling and structural analysis shown
additional information
-
studies on architecture and potential roles of the C-terminal accessory domain in structural and functional protein regulation performed, conformational changes during the catalytic cycle of the ATPase unit of OpuA protein determined, single cysteine mutants generated, static and time-resolved FRET measurements applied, molecular modelling and structural analysis shown
additional information
-
protective effects of glycine betaine on the survival of Listeria monocytogenes on leaf surfaces studied, mutants carrying deletions in glycine betaine uptake systems analyzed, inoculation of leaves described, enumeration of bacterial populations determined, statistical analysis performed
additional information
osmoprotection assays and transport assays applied, kinetic studies with radiolabeled substrates performed, OpuC identified as sole transporter for glycine betaine and as one of multiple transporters for choline under high osmolarity, close relation to OpuC transporters of Bacillus subtilis and Listeria monocytogenes determined, cystathionine-beta-synthase domain identification and homology search performed
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 35
-
10°C: about 45% of maximal activity, 35°C: about 55% of maximal activity, at 30 mM KCl
15 - 40
-
about 45% of maximal activity at 15°C and at 40°C, at 600 mM sucrose
37 - 52
-
reduced growth rate at higher temperatures, addition of 1 mM glycine betaine, homobetaine, carnitine, butyrobetaine, crotonobetaine, DMSP, choline, or glutamate have a clear thermoprotective effect at 52°C, heat protectants are taken up under heat stress via the OpuA, OpuC, and OpuD transporters, despite the strongly reduced glycine betaine transport rate at 52°C, substantial glycine betaine accumulation, but it is not increased in comparison to cells grown at 37°C, thermoprotection by glutamate does not depend on an increased cellular pool of this amino acid
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
opuA operon, genes opuAA, opuAB, and opuAC encoding glycine betaine transport ATP-binding protein OpuAA (quaternary-amine-transporting ATPase), glycine betaine transport system permease protein OpuAB, and glycine betaine-binding protein OpuAC
U5LFB4; U5LHK3; U5LHN4
UniProt
brenda
ATP-binding protein, gene PSPTO4575, OpuCA; pv. tomato, strain DC3000
SwissProt
brenda
Vibrio anguillarum serotype O1 MVM425
opuA operon, genes opuAA, opuAB, and opuAC encoding glycine betaine transport ATP-binding protein OpuAA (quaternary-amine-transporting ATPase), glycine betaine transport system permease protein OpuAB, and glycine betaine-binding protein OpuAC
U5LFB4; U5LHK3; U5LHN4
UniProt
brenda
gene opuAB encoding glycine betaine transport system permease protein OpuAB
UniProt
brenda
glycine betaine transport system permease protein OpuAB
UniProt
brenda
three transport systems for the osmoprotectant glycine betaine: OpuA, OpuC and Opu D
-
-
brenda
wild-type strain JH642, mutant strains RMKB24, RMKB34, RMKB22, and RMKB33
-
-
brenda
gene opuAB encoding glycine betaine transport system permease protein OpuAB
UniProt
brenda
glycine betaine transport system permease protein OpuAB
UniProt
brenda
glycine betaine transport system permease protein OpuAB
UniProt
brenda
derivatives, cultivated on leaf surface of Petroselinum sativum
-
-
brenda
derivatives, cultivated on leaf surface of Petroselinum sativum
-
-
brenda
genes proW and proX encoding ABC transporter permease and choline ABC transporter substrate-binding protein (glycine/betaine ABC transporter substrate-binding protein), respectively; isolated from diseased fish suffered from epidemic vibriosis in the fishery in the Northern China Sea
A0A097A5F2; A0A077T7R8
UniProt
brenda
genes proW, proX, and proV encoding glycine betaine transporter membrane protein (proline/betaine ABC transporter permease), glycine betaine ABC transporter substrate-binding protein, and glycine betaine/L-proline ABC transporter ATP-binding protein, respectively; isolated from diseased fish suffered from epidemic vibriosis in the fishery in the Northern China Sea
A0A077T980; A0A077T7U5; A0A077T7Z1
UniProt
brenda
Vibrio anguillarum serotype O1 MVM425
genes proW and proX encoding ABC transporter permease and choline ABC transporter substrate-binding protein (glycine/betaine ABC transporter substrate-binding protein), respectively; isolated from diseased fish suffered from epidemic vibriosis in the fishery in the Northern China Sea
A0A097A5F2; A0A077T7R8
UniProt
brenda
Vibrio anguillarum serotype O1 MVM425
genes proW, proX, and proV encoding glycine betaine transporter membrane protein (proline/betaine ABC transporter permease), glycine betaine ABC transporter substrate-binding protein, and glycine betaine/L-proline ABC transporter ATP-binding protein, respectively; isolated from diseased fish suffered from epidemic vibriosis in the fishery in the Northern China Sea
A0A077T980; A0A077T7U5; A0A077T7Z1
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
OpuAA, a nucleotide binding protein of the OpuA transporter
brenda
-
the solute ABC transporter has a substrate-binding protein fused to the transmembrane domain
brenda
-
the solute ABC transporter has a substrate-binding protein fused to the transmembrane domain
brenda
-
transmembrane domain fused to the substrate-binding domain
brenda
-
the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit is located close to the membrane surface, where its hydrophobic face interacts with the transport protein rather than the membrane lipids. The amphipathic alpha-helix of OpuA is necessary for high activity of OpuA but is not critical for the biogenesis of the protein or the ionic regulation of transport
brenda
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
OpuF is a member of the Opu family of transporters. OpuF is not present in Bacillus subtilis but it is widely distributed in members of the large Bacillus genus. OpuF is a representative of a sub-group of ABC transporters in which the substrate-binding protein (SBP) is fused to the trans-locating subunit (TMD). The OpuF system is a representative of a growing sub-group of ABC transporters in which the substrate-scavenging function of the SBP and the membrane-embedded substrate TMD are fused into a single polypeptide chain
evolution
-
OpuF is a member of the Opu family of transporters. OpuF is widely distributed in members of the large Bacillus genus. OpuF is a representative of a sub-group of ABC transporters in which the substrate-binding protein (SBP) is fused to the trans-locating subunit (TMD). The OpuF system is a representative of a growing sub-group of ABC transporters in which the substrate-scavenging function of the SBP and the membrane-embedded substrate TMD are fused into a single polypeptide chain
evolution
the amino acid sequences of the components of Bacillus subtilis OpuB and OpuC ABC transporters are closely related to each other because the opuB and opuC operon are likely the result of a gene duplication event. The least conserved component of these two transporter systems are their substrate binding proteins (OpuBC and OpuCC, respectively) with a degree of amino acid sequence identity of 71% of the mature proteins. Gene opuAA (UniProt ID O32243) encodes the glycine betaine transport ATP-binding protein OpuAA (quaternary-amine-transporting ATPase)
evolution
the amino acid sequences of the components of Bacillus subtilis OpuB and OpuC ABC transporters are closely related to each other because the opuB and opuC operon are likely the result of a gene duplication event. The least conserved component of these two transporter systems are their substrate binding proteins (OpuBC and OpuCC, respectively) with a degree of amino acid sequence identity of 71% of the mature proteins. Gene opuAA (UniProt ID O32243) encodes the glycine betaine transport ATP-binding protein OpuAA (quaternary-amine-transporting ATPase). OpuA-type ABC transporters are identified by assessing the amino acid sequence relatedness with the OpuAC substrate-binding protein from Bacillus subtilis
evolution
U5LFB4; U5LHK3; U5LHN4
the genome sequence of Bacillus infantis NRRL B-14911 predicts in addition to OpuA, the presence of several other types of osmostress protectant uptake systems (e.g. OpuF, OpuD, OpuE)
evolution
the structural genes encoding ABC-transporters OpuB and OpuC from Bacillus subtilis have most likely evolved through a duplication event but the two transporters are remarkably different in their substrate profile. The transporters are members of the type-I subfamily of ABC import systems. The substrate-binding protein-dependent ABC systems are all thought to be importers and probably originated from a common ancestor more than 3 billion years ago
evolution
-
the amino acid sequences of the components of Bacillus subtilis OpuB and OpuC ABC transporters are closely related to each other because the opuB and opuC operon are likely the result of a gene duplication event. The least conserved component of these two transporter systems are their substrate binding proteins (OpuBC and OpuCC, respectively) with a degree of amino acid sequence identity of 71% of the mature proteins. Gene opuAA (UniProt ID O32243) encodes the glycine betaine transport ATP-binding protein OpuAA (quaternary-amine-transporting ATPase). OpuA-type ABC transporters are identified by assessing the amino acid sequence relatedness with the OpuAC substrate-binding protein from Bacillus subtilis
-
evolution
-
the structural genes encoding ABC-transporters OpuB and OpuC from Bacillus subtilis have most likely evolved through a duplication event but the two transporters are remarkably different in their substrate profile. The transporters are members of the type-I subfamily of ABC import systems. The substrate-binding protein-dependent ABC systems are all thought to be importers and probably originated from a common ancestor more than 3 billion years ago
-
evolution
-
the amino acid sequences of the components of Bacillus subtilis OpuB and OpuC ABC transporters are closely related to each other because the opuB and opuC operon are likely the result of a gene duplication event. The least conserved component of these two transporter systems are their substrate binding proteins (OpuBC and OpuCC, respectively) with a degree of amino acid sequence identity of 71% of the mature proteins. Gene opuAA (UniProt ID O32243) encodes the glycine betaine transport ATP-binding protein OpuAA (quaternary-amine-transporting ATPase)
-
evolution
-
the genome sequence of Bacillus infantis NRRL B-14911 predicts in addition to OpuA, the presence of several other types of osmostress protectant uptake systems (e.g. OpuF, OpuD, OpuE)
-
evolution
-
the structural genes encoding ABC-transporters OpuB and OpuC from Bacillus subtilis have most likely evolved through a duplication event but the two transporters are remarkably different in their substrate profile. The transporters are members of the type-I subfamily of ABC import systems. The substrate-binding protein-dependent ABC systems are all thought to be importers and probably originated from a common ancestor more than 3 billion years ago
-
malfunction
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
in-frame deletion mutation in the two putative ABC transporters and three putative BCCT family transporters associated with glycine betaine uptake cannot block cellular accumulation of betaine glycine in Vibrio anguillarum under cold stress, suggesting the redundant feature in Vibrio anguillarum betaine transporter system
malfunction
OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional
malfunction
OpuC transporter lacking its solute receptor protein OpuCC is nonfunctional
malfunction
-
OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional
-
malfunction
-
OpuC transporter lacking its solute receptor protein OpuCC is nonfunctional
-
malfunction
Vibrio anguillarum serotype O1 MVM425
-
in-frame deletion mutation in the two putative ABC transporters and three putative BCCT family transporters associated with glycine betaine uptake cannot block cellular accumulation of betaine glycine in Vibrio anguillarum under cold stress, suggesting the redundant feature in Vibrio anguillarum betaine transporter system
-
malfunction
-
OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional
-
malfunction
-
OpuC transporter lacking its solute receptor protein OpuCC is nonfunctional
-
physiological function
-
strains lacking opuABCD accumulate more trehalose under stress conditions than wild-type strains. OpuABCD mutant strains are more resistant to high-salt, low-pH and -hydrogen peroxide, conditions that mimic aspects of innate immunity, in a trehalose-dependent manner. In addition, OpuABCD mutant strains require the trehalose production genes to outcompete wild-type strains in mice and macrophages
physiological function
-
the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit is located close to the membrane surface, where its hydrophobic face interacts with the transport protein rather than the membrane lipids. The amphipathic alpha-helix of OpuA is necessary for high activity of OpuA but is not critical for the biogenesis of the protein or the ionic regulation of transport
physiological function
-
the enzyme ontributes to the regulation of cell volume
physiological function
five transporters for osmostress protectants (Opu) have been characterized in the systems for production of the compatible solutes proline and glycine betaine. Glycine betaine synthesis relies on the import of choline via the substrate-restricted OpuB system and the promiscuous OpuC transporter and its subsequent oxidation by the GbsAB enzymes. Transcription of the opuB and gbsAB operons is under control of the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor. GbsR-/OpuAR-type proteins are an extended subgroup within the MarR-superfamily of transcriptional regulators and an additional type of substrate-inducible import system for osmostress protectants. The presence of either glycine betaine or proline betaine affords a substantial level of osmostress protection. Choline serves as the inducer for relief of GbsR-mediated repression of the Bacillus subtilis gbsAB and opuB operons
physiological function
five transporters for osmostress protectants (Opu) have been characterized in the systems for production of the compatible solutes proline and glycine betaine. Glycine betaine synthesis relies on the import of choline via the substrate-restricted OpuB system and the promiscuous OpuC transporter and its subsequent oxidation by the GbsAB enzymes. Transcription of the opuB and gbsAB operons is under control of the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor. GbsR-/OpuAR-type proteins are an extended subgroup within the MarR-superfamily of transcriptional regulators and an additional type of substrate-inducible import system for osmostress protectants. The presence of either glycine betaine or proline betaine affords a substantial level of osmostress protection. Since the genome sequence of Bacillus infantis NRRL B-14911 lacks glycine betaine synthesis genes, it is readily understandable why choline is not osmostress protective, as this compound is not a compatible solute per se because its osmostress-relieving properties depend on its enzymatic conversion into glycine betaine
physiological function
U5LFB4; U5LHK3; U5LHN4
five transporters for osmostress protectants (Opu) have been characterized in the systems for production of the compatible solutes proline and glycine betaine. Glycine betaine synthesis relies on the import of choline via the substrate-restricted OpuB system and the promiscuous OpuC transporter and its subsequent oxidation by the GbsAB enzymes. Transcriptional regulation of the Bacillus infantis opuA gene cluster via the GbsR-type regulator OpuAR, the Bacillus infantis GbsR protein is the OpuAR regulatory protein. GbsR-/OpuAR-type proteins are an extended subgroup within the MarR-superfamily of transcriptional regulators and an additional type of substrate-inducible import system for osmostress protectants. The presence of either glycine betaine or proline betaine affords a substantial level of osmostress protection. The major substrates (glycine betaine and proline betaine) of Bacillus infantis OpuA ABC importer also serve as inducers of OpuAR to relieve the DNA-binding activity of this repressor protein
physiological function
-
OpuF is another Bacillus compatible solute ABC transporter with a substrate-binding protein fused to the transmembrane domain. OpuF mediates the import of glycine betaine, proline betaine, homobetaine and the marine osmolyte dimethylsulfoniopropionate (DMSP). The high affinity import of compatible solutes from environmental sources is an important aspect of the cellular defense of many Bacteria and Archaea against the harmful effects of high external osmolarity. The accumulation of these osmostress protectants counteracts high osmolarity instigated water efflux, drop in turgor to non-physiological values, and an undue increase in molecular crowding of the cytoplasm, they thereby foster microbial growth under osmotically unfavorable conditions
physiological function
-
OpuF is another Bacillus compatible solute ABC transporter with a substrate-binding protein fused to the transmembrane domain. OpuF mediates the import of glycine betaine, proline betaine, homobetaine and the marine osmolyte dimethylsulfoniopropionate (DMSP). The high affinity import of compatible solutes from environmental sources is an important aspect of the cellular defense of many Bacteria and Archaea against the harmful effects of high external osmolarity. The accumulation of these osmostress protectants counteracts high osmolarity instigated water efflux, drop in turgor to non-physiological values, and an undue increase in molecular crowding of the cytoplasm, they thereby foster microbial growth under osmotically unfavorable conditions
physiological function
the ABC-transporters OpuB and OpuC from Bacillus subtilis function as osmoprotectant import systems. OpuB possesses narrow substrate specificity, while OpuC is promiscuous. Critical role of the binding protein OpuBC (UniProt ID Q45462) in setting the substrate specificity of ABC transporter. OpuABC, consisting of ATPase OpuBA and substrate-binding-protein OpuBC, acts as an osmoprotectant uptake system. A central role is played by the extra-cytoplasmic ligand-binding protein for the overall functioning of these importer systems. Osmostress protection under high-salinity growth conditions and import of various compatible solutes via the OpuB, OpuC, OpuB::OpuCC, and OpuC::OpuBC ABC transport systems, overview. GbsR-dependent regulation of opuB and gbsAB (glycine betaine biosynthetic gene cluster) expression
physiological function
the ABC-transporters OpuB and OpuC from Bacillus subtilis function as osmoprotectant import systems. OpuB possesses narrow substrate specificity, while OpuC is promiscuous. Critical role of the binding protein OpuCC (UniProt ID O32243) in setting the substrate specificity of ABC transporter. OpuACC, consisting of ATPase OpuCA and substrate-binding-protein OpuCC, acts as an osmoprotectant uptake system. A central role is played by the extra-cytoplasmic ligand-binding protein for the overall functioning of these importer systems. Osmostress protection under high-salinity growth conditions and import of various compatible solutes via the OpuB, OpuC, OpuB::OpuCC, and OpuC::OpuBC ABC transport systems, overview
physiological function
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
Vibrio anguillarum possesses a putative glycine betaine synthesis system, which is encoded by betABI and synthesizes glycine betaine from its precursor choline. Significant up-regulation of the bet gene at the transcriptional level is noted in log phase in response to cold-stress. The accumulation of betaine glycine is only appearing at low growth temperatures, suggesting that response regulation of both synthesis system and transporter system are cold-dependent. Two putative ABC transporters and three putative BCCT family transporters are associated with glycine betaine uptake. Glycine betaine serves as an effective cold stress protectant, thus the enzyme complex is involved in cold adaptation of Vibrio anguillarum via regulation of the glycine betaine level
physiological function
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
Vibrio anguillarum possesses a putative glycine betaine synthesis system, which is encoded by betABI and synthesizes glycine betaine from its precursor choline. Significant upregulation of the bet gene at the transcriptional level is noted in log phase in response to cold-stress. The accumulation of betaine glycine is only appearing at low growth temperatures, suggesting that response regulation of both synthesis system and transporter system are cold-dependent. Two putative ABC transporters and three putative BCCT family transporters are associated with glycine betaine uptake. Glycine betaine serves as an effective cold stress protectant, thus the enzyme complex is involved in cold adaptation of Vibrio anguillarum via regulation of the glycine betaine level
physiological function
-
five transporters for osmostress protectants (Opu) have been characterized in the systems for production of the compatible solutes proline and glycine betaine. Glycine betaine synthesis relies on the import of choline via the substrate-restricted OpuB system and the promiscuous OpuC transporter and its subsequent oxidation by the GbsAB enzymes. Transcription of the opuB and gbsAB operons is under control of the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor. GbsR-/OpuAR-type proteins are an extended subgroup within the MarR-superfamily of transcriptional regulators and an additional type of substrate-inducible import system for osmostress protectants. The presence of either glycine betaine or proline betaine affords a substantial level of osmostress protection. Choline serves as the inducer for relief of GbsR-mediated repression of the Bacillus subtilis gbsAB and opuB operons
-
physiological function
-
the ABC-transporters OpuB and OpuC from Bacillus subtilis function as osmoprotectant import systems. OpuB possesses narrow substrate specificity, while OpuC is promiscuous. Critical role of the binding protein OpuBC (UniProt ID Q45462) in setting the substrate specificity of ABC transporter. OpuABC, consisting of ATPase OpuBA and substrate-binding-protein OpuBC, acts as an osmoprotectant uptake system. A central role is played by the extra-cytoplasmic ligand-binding protein for the overall functioning of these importer systems. Osmostress protection under high-salinity growth conditions and import of various compatible solutes via the OpuB, OpuC, OpuB::OpuCC, and OpuC::OpuBC ABC transport systems, overview. GbsR-dependent regulation of opuB and gbsAB (glycine betaine biosynthetic gene cluster) expression
-
physiological function
-
five transporters for osmostress protectants (Opu) have been characterized in the systems for production of the compatible solutes proline and glycine betaine. Glycine betaine synthesis relies on the import of choline via the substrate-restricted OpuB system and the promiscuous OpuC transporter and its subsequent oxidation by the GbsAB enzymes. Transcription of the opuB and gbsAB operons is under control of the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor. GbsR-/OpuAR-type proteins are an extended subgroup within the MarR-superfamily of transcriptional regulators and an additional type of substrate-inducible import system for osmostress protectants. The presence of either glycine betaine or proline betaine affords a substantial level of osmostress protection. Since the genome sequence of Bacillus infantis NRRL B-14911 lacks glycine betaine synthesis genes, it is readily understandable why choline is not osmostress protective, as this compound is not a compatible solute per se because its osmostress-relieving properties depend on its enzymatic conversion into glycine betaine
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physiological function
-
the ABC-transporters OpuB and OpuC from Bacillus subtilis function as osmoprotectant import systems. OpuB possesses narrow substrate specificity, while OpuC is promiscuous. Critical role of the binding protein OpuCC (UniProt ID O32243) in setting the substrate specificity of ABC transporter. OpuACC, consisting of ATPase OpuCA and substrate-binding-protein OpuCC, acts as an osmoprotectant uptake system. A central role is played by the extra-cytoplasmic ligand-binding protein for the overall functioning of these importer systems. Osmostress protection under high-salinity growth conditions and import of various compatible solutes via the OpuB, OpuC, OpuB::OpuCC, and OpuC::OpuBC ABC transport systems, overview
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physiological function
Vibrio anguillarum serotype O1 MVM425
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Vibrio anguillarum possesses a putative glycine betaine synthesis system, which is encoded by betABI and synthesizes glycine betaine from its precursor choline. Significant upregulation of the bet gene at the transcriptional level is noted in log phase in response to cold-stress. The accumulation of betaine glycine is only appearing at low growth temperatures, suggesting that response regulation of both synthesis system and transporter system are cold-dependent. Two putative ABC transporters and three putative BCCT family transporters are associated with glycine betaine uptake. Glycine betaine serves as an effective cold stress protectant, thus the enzyme complex is involved in cold adaptation of Vibrio anguillarum via regulation of the glycine betaine level
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physiological function
Vibrio anguillarum serotype O1 MVM425
-
Vibrio anguillarum possesses a putative glycine betaine synthesis system, which is encoded by betABI and synthesizes glycine betaine from its precursor choline. Significant up-regulation of the bet gene at the transcriptional level is noted in log phase in response to cold-stress. The accumulation of betaine glycine is only appearing at low growth temperatures, suggesting that response regulation of both synthesis system and transporter system are cold-dependent. Two putative ABC transporters and three putative BCCT family transporters are associated with glycine betaine uptake. Glycine betaine serves as an effective cold stress protectant, thus the enzyme complex is involved in cold adaptation of Vibrio anguillarum via regulation of the glycine betaine level
-
physiological function
-
five transporters for osmostress protectants (Opu) have been characterized in the systems for production of the compatible solutes proline and glycine betaine. Glycine betaine synthesis relies on the import of choline via the substrate-restricted OpuB system and the promiscuous OpuC transporter and its subsequent oxidation by the GbsAB enzymes. Transcriptional regulation of the Bacillus infantis opuA gene cluster via the GbsR-type regulator OpuAR, the Bacillus infantis GbsR protein is the OpuAR regulatory protein. GbsR-/OpuAR-type proteins are an extended subgroup within the MarR-superfamily of transcriptional regulators and an additional type of substrate-inducible import system for osmostress protectants. The presence of either glycine betaine or proline betaine affords a substantial level of osmostress protection. The major substrates (glycine betaine and proline betaine) of Bacillus infantis OpuA ABC importer also serve as inducers of OpuAR to relieve the DNA-binding activity of this repressor protein
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physiological function
-
the ABC-transporters OpuB and OpuC from Bacillus subtilis function as osmoprotectant import systems. OpuB possesses narrow substrate specificity, while OpuC is promiscuous. Critical role of the binding protein OpuBC (UniProt ID Q45462) in setting the substrate specificity of ABC transporter. OpuABC, consisting of ATPase OpuBA and substrate-binding-protein OpuBC, acts as an osmoprotectant uptake system. A central role is played by the extra-cytoplasmic ligand-binding protein for the overall functioning of these importer systems. Osmostress protection under high-salinity growth conditions and import of various compatible solutes via the OpuB, OpuC, OpuB::OpuCC, and OpuC::OpuBC ABC transport systems, overview. GbsR-dependent regulation of opuB and gbsAB (glycine betaine biosynthetic gene cluster) expression
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physiological function
-
the ABC-transporters OpuB and OpuC from Bacillus subtilis function as osmoprotectant import systems. OpuB possesses narrow substrate specificity, while OpuC is promiscuous. Critical role of the binding protein OpuCC (UniProt ID O32243) in setting the substrate specificity of ABC transporter. OpuACC, consisting of ATPase OpuCA and substrate-binding-protein OpuCC, acts as an osmoprotectant uptake system. A central role is played by the extra-cytoplasmic ligand-binding protein for the overall functioning of these importer systems. Osmostress protection under high-salinity growth conditions and import of various compatible solutes via the OpuB, OpuC, OpuB::OpuCC, and OpuC::OpuBC ABC transport systems, overview
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additional information
-
an in silico model of the substrate-binding protein (SBP) domain of the transmembrane domain (TMD)-SPB hybrid protein OpuFB is established. It reveals the presence of an aromatic cage, a structural feature commonly present in ligand-binding sites of compatible solute importers
additional information
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an in silico model of the substrate-binding protein (SBP) domain of the transmembrane domain (TMD)-SPB hybrid protein OpuFB is established. It reveals the presence of an aromatic cage, a structural feature commonly present in ligand-binding sites of compatible solute importers
Show AA Sequence and Transmembrane Helices (1628 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45679
-
x * 45679, BusAA + x * 61966, BusAB + x * ?, BusAC, calculation from nucleotide sequence
61966
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x * 45679, BusAA + x * 61966, BusAB + x * ?, BusAC, calculation from nucleotide sequence
additional information
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the OpuA component of the wild-type enzyme runs at a lower molecular weight than that of W484C and the substrate binding domain-less mutant
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
nucleotide-binding protein domain, displays lower ATPase activity than the dimeric form
monomer
additional information
?
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x * 45679, BusAA + x * 61966, BusAB + x * ?, BusAC, calculation from nucleotide sequence
?
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x * 45679, BusAA + x * 61966, BusAB + x * ?, BusAC, calculation from nucleotide sequence
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monomer
-
nucleotide-binding protein domain, displays higher ATPase activity than the dimeric form
additional information
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the transport system consists of an ATPase, OpuAA, an integral membrane protein OpuAB and a hydrophilic polypeptide OpuAC
additional information
the ABC transporter protein complex comprises the nucleotide-binding domain (NBD) and transmembrane domain (TMD) core components, and an extra-cytoplasmic ligand-binding protein, close structural relationship of the components of the OpuB and OpuC systems
additional information
the ABC transporter protein complex comprises the nucleotide-binding domain (NBD) and transmembrane domain (TMD) core components, and an extra-cytoplasmic ligand-binding protein, close structural relationship of the components of the OpuB and OpuC systems
additional information
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the ABC transporter protein complex comprises the nucleotide-binding domain (NBD) and transmembrane domain (TMD) core components, and an extra-cytoplasmic ligand-binding protein, close structural relationship of the components of the OpuB and OpuC systems
additional information
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the ABC transporter protein complex comprises the nucleotide-binding domain (NBD) and transmembrane domain (TMD) core components, and an extra-cytoplasmic ligand-binding protein, close structural relationship of the components of the OpuB and OpuC systems
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additional information
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the ABC transporter protein complex comprises the nucleotide-binding domain (NBD) and transmembrane domain (TMD) core components, and an extra-cytoplasmic ligand-binding protein, close structural relationship of the components of the OpuB and OpuC systems
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additional information
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the periplasmic glycine betaine binding protein has a MW of 31000 Da as determined by SDS-PAGE and 35000 Da as determined by gel filtration
additional information
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the glycine betaine transport system consitsts of an ATP-binding/hydrolyzing subunit, OpuAAA and a protein OpuABC that contains both the translocator and the substrate binding domain. The enzyme is composed of five proteins or domains
additional information
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the glycine betaine transport system consitsts of an ATP-binding/hydrolyzing subunit, OpuAAA and a protein OpuABC that contains both the translocator and the substrate binding domain. The enzyme is composed of five proteins or domains
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
lipoprotein
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strong indication that OpuAC is a lipoprotein with an amino-terminal Cys-lipid anchor for the mature protein
lipoprotein
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OpuA is a lipoprotein, the lipidless OpuAC-3 protein is held in the cytoplasmic membrane of Bacillus subtilis via its uncleaved hydrophobic signal peptide
lipoprotein
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strong indication that OpuAC is a lipoprotein with an amino-terminal Cys-lipid anchor for the mature protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
OpuBC protein crystal structure analysis, PDB ID 3R6U
U5LFB4; U5LHK3; U5LHN4
by hanging-drop method, structures of substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution, structures show a substrate-binding protein-dependent-typical class II fold, structural differences of complexes occur within the ligand-binding pocket as well as across the domain-domain interface, explaining the differences in affinity of the substrate-binding domain-glycine betaine complex with KD = 0.017 mM, and substrate-binding domain-proline betaine complex with KD = 0.295 mM
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substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution
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substrate-binding protein OpuBC in complex with choline, to 1.6 A resolution. The positively charged trimethylammonium head group of choline is wedged into an aromatic cage formed by four tyrosine residues and is bound via cation-pi interactions. The hydroxyl group of choline protrudes out of this aromatic cage and makes a single interaction with residue Gln19. A water network stabilizes choline within its substrate-binding site and promotes indirect interactions between the two lobes of the OpuBC protein. Disruption of this intricate water network strongly reduces choline binding affinity or abrogates ligand binding
substrate-binding protein OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine to 2.3, 2.7, 2.4, 1.9 and 2.1 A resolution, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with a substrate-binding pocket located at the interdomain cleft. Upon substrate binding, the two domains shift towards each other to trap the substrate
crystallization in an open and closed-liganded conformation, to 1.9 and 2.3 A resolution, respectively. Solutes like proline and carnitine bind with affinities that are 3 to 4 orders of magnitude lower than affinities of substrates glycine betaine or proline betaine. The low affinity substrates are not noticeably transported by membrane-reconstituted OpuA. The binding pocket is formed by three tryptophans coordinating the quaternary ammonium group of glycine betaine in the closed-liganded structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D149A/L155A
decrease in choline binding affinity by approximately 38fold
E171Q
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the monomer is the preferred species for the nucleotide-free state in solution
G161C
single cysteine mutants generated by site-directed mutagenesis
S171C
single cysteine mutants generated by site-directed mutagenesis
T94D
shares a quite similar pattern of fluorescence spectrum to that of the paralogue OpuBC. Only choline can trigger obvious changes of fluorescence intensity of mutant T94D, whereas carnitine, GB and ectoine cannot
S24C
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mutations in the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit. Mutation does not have distant structural effects on the overall conformation of the transporter
T23C
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mutations in the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit. Mutation does not have distant structural effects on the overall conformation of the transporter
T25C
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mutations in the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit. Mutation does not have distant structural effects on the overall conformation of the transporter
W484C
additional information
W484C
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mutant with 10fold increased KM for glycine betaine than the wild type enzyme
W484C
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mutant with 10fold increased KM for glycine betaine than the wild type enzyme
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additional information
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deletion of the various Opu transport systems prevents thermoprotection by compatible solutes
additional information
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mutant strain RMKB24, lacking OpuA, OpuC, and OpuD, is not protected by glycine betaine from the detrimental effects of high temperature, mutant strains RMKB34, RMKB22, and RMKB33, which express only one of the glycine betaine transporters, are protected from heat stress
additional information
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuC. The hybrid OpuB::OpuCC transporter is inefficient to relieve osmotic stress. De-repression of transcription of the opuB::opuCC operon is responsible for enhanced growth of the suppressor mutants at high salinity
additional information
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuC. The hybrid OpuB::OpuCC transporter is inefficient to relieve osmotic stress. De-repression of transcription of the opuB::opuCC operon is responsible for enhanced growth of the suppressor mutants at high salinity
additional information
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construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuC. The hybrid OpuB::OpuCC transporter is inefficient to relieve osmotic stress. De-repression of transcription of the opuB::opuCC operon is responsible for enhanced growth of the suppressor mutants at high salinity
additional information
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
additional information
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
additional information
-
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
additional information
-
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuC. The hybrid OpuB::OpuCC transporter is inefficient to relieve osmotic stress. De-repression of transcription of the opuB::opuCC operon is responsible for enhanced growth of the suppressor mutants at high salinity
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additional information
-
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
-
additional information
-
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuC. The hybrid OpuB::OpuCC transporter is inefficient to relieve osmotic stress. De-repression of transcription of the opuB::opuCC operon is responsible for enhanced growth of the suppressor mutants at high salinity
-
additional information
-
construction of hybrids between the two ABC-transporters OpuB and OpuC from Bacillus subtilis by reciprocally exchanging the coding regions for the OpuBC and OpuCC substrate-binding proteins between the corresponding opuB and opuC operons resulting in strains TMB118 and LTB1. Exchanging the binding protein between the two ABC transporters inverses the substrate specificity, OpuB::OpuCC turns into a promiscuous system, while OpuC::OpuBC now exhibits narrow substrate specificity, each in contrast to the wild-type. Both hybrid transporters possess a high affinity for their substrates but the transport capacity of the OpuB::OpuCC system is moderate due to the synthesis of only low amounts of the xenogenetic OpuCC protein. Suppressor mutations causing single amino acid substitutions in the GbsR repressor controlling the choline to glycine betaine biosynthesis pathway greatly improve OpuB::OpuCC-mediated compatible solute import through transcriptional up-regulation of the hybrid opuB::opuCC operon. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
-
additional information
OpuAdelta12, anionic tail deletion mutant, Rb+ and Cs+ no longer inhibitory, more K+ needed for activation than for the wild-type
additional information
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OpuAdelta12, anionic tail deletion mutant, Rb+ and Cs+ no longer inhibitory, more K+ needed for activation than for the wild-type
additional information
-
deletion of the amphipathic alpha-helix inactivates OpuA. Deleting part of the helix but leaving the amino-terminus and linker region intact results in a major decrease in activity. The amphipathic alpha-helix is critical for maximal activity but not for the ionic regulation of the transporter
additional information
-
OpuAdelta12, anionic tail deletion mutant, Rb+ and Cs+ no longer inhibitory, more K+ needed for activation than for the wild-type
-
additional information
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mutants LO28deltaB, LO28deltaC, LO28deltaG, LO28deltaBG, LO28deltaCG, LO28deltaBCG, LO28deltaBCGsoe, LO28deltaBCGB, deletion of osmolyte transporters reduces growth at low temperatures
additional information
-
mutants LO28deltaB, LO28deltaC, LO28deltaG, LO28deltaBG, LO28deltaCG, LO28deltaBCG, LO28deltaBCGsoe, LO28deltaBCGB, deletion of osmolyte transporters reduces growth at low temperatures
-
additional information
deletion mutants of OpuC generated, complementation of deletion mutants shown
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme is activated by decreasing temperature within the range of 15°C to 4°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography and size-exclusion chromatography of solubilized membrane fractions
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isolated transmembrane subunits purified by Strep-tag affinity purification
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OpuAA, purified to homogeneity, affinity chromatography and gel filtration
-
recombinant wild-type and mutant OpuAR repressor proteins from Escherichia coli strain BL21 by affinity chromatography and gel filtration, determination of quaternary assembly of purified OpuAR protein
U5LFB4; U5LHK3; U5LHN4
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into pApBetT, transfered to Escherichia coli and then to MKH13 cells, overexpression in freshwater Synechococcus sp. strain PCC7942 cells
expressed in Escherichia coli, cysteine mutants generated and inserted into pBAD33
expressed in Escherichia coli, DH5-alpha used as host for cloning, MG1655 used as host for mutagenesis
expression in Escherichia coli
gene opuF, functional expression and resonstitution of the OpuF transporter in Bacillus subtilis
genes proW and proX are located on chromosome 2 (Vibrio anguillarum strain MVM425 genome is composed of two circular chromosomes) and encode ABC transporter permease and choline ABC transporter substrate-binding protein (glycine/betaine ABC transporter substrate-binding protein), respectively, DNA and amino acid sequence determination and analyis, sequence comparisons, quantitative real-time RT-PCR expression analysis
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
genes proW, proX, and proV are located on chromosome 2 (Vibrio anguillarum strain MVM425 genome is composed of two circular chromosomes) and encode glycine betaine transporter membrane protein (proline/betaine ABC transporter permease), glycine betaine ABC transporter substrate-binding protein, and glycine betaine/L-proline ABC transporter ATP-binding protein, respectively, DNA and amino acid sequence determination and analyis, sequence comparisons, quantitative real-time RT-PCR expression analysis
A0A077T980; A0A077T7U5; A0A077T7Z1, A0A097A5F2; A0A077T7R8
nucleotide-binding protein domain cloned as an N- or C-terminal His-tagged fusion protein and overexpressed in Escherichia coli BL21 (DE3) under the control of an arabinose-inducible promoter, overexpression of the transmembrane domain only possible in Walker strains BL21(DE3)C41 and C43 under the control of an ITPG- or arabinose-inducible promoter as N- and C-terminal His- and Strep-tagged versions
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opuA operon, the coding region of the opuA operon and the adjacent opuAR regulatory gene are cloned into the vector pX resulting in plasmid pCA-opuARA, sequence comparisons, recombinant expression in Bacillus subtilis strain TMB118, in which only the proline-specific osmostress OpuE transporter is present, the resulting strain is CAB2. opuAA0 Bacillus infantis-treA reporter gene fusions are constructed using primers opuAR treA Frag1/2 rev and either opuAR treA Frag1/4. Recombinant overexpression of StrepII-tagged OpuAR repressor and mutant derivatives from the P-tet promoter in the Escherichia coli B strain BL21
U5LFB4; U5LHK3; U5LHN4
substrate-binding domain into vector pBKB76, expression in Escherichia coli BL21 (DE3)
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transmembrane subunits cloned into vector pBAD33 or pET21a, expression in Escherichia coli
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gene opuF, functional expression and resonstitution of the OpuF transporter in Bacillus subtilis
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gene opuF, functional expression and resonstitution of the OpuF transporter in Bacillus subtilis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced in response to an osmotic upshock and sustained high salinity
the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor, controls the transcription of the opuB and gbsAB operons
the trans-acting regulatory gene gbsR encodes a repressor (GbsR) for the opuB operon
enzyme expression is induced in response to an osmotic upshock and sustained high salinity
-
enzyme expression is induced in response to an osmotic upshock and sustained high salinity
-
-
the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor, controls the transcription of the opuB and gbsAB operons
the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor, controls the transcription of the opuB and gbsAB operons
U5LFB4; U5LHK3; U5LHN4
the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor, controls the transcription of the opuB and gbsAB operons
-
-
the MarR-type regulator GbsR, which acts as an intracellular choline-responsive repressor, controls the transcription of the opuB and gbsAB operons
-
-
the trans-acting regulatory gene gbsR encodes a repressor (GbsR) for the opuB operon
the trans-acting regulatory gene gbsR encodes a repressor (GbsR) for the opuB operon
-
-
the trans-acting regulatory gene gbsR encodes a repressor (GbsR) for the opuB operon
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
functional expression and resonstitution of the OpuF transporter in Bacillus subtilis
functional expression and resonstitution of the OpuF transporter in Bacillus subtilis
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functional expression and resonstitution of the OpuF transporter in Bacillus subtilis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
additional information
molecular biology
-
opuC gene is transcribed exclusively from a sigmaB-dependent promoter, transcripts originating from the sigmaB-dependent opuC accumulate substantially after osmotic upshift but are minimal after temperature upshift or ethanol stress
molecular biology
-
opuC gene is transcribed exclusively from a sigmaB-dependent promoter, transcripts originating from the sigmaB-dependent opuC accumulate substantially after osmotic upshift but are minimal after temperature upshift or ethanol stress
-
additional information
-
betaine and carnitine transport upon low temperature exposure is mediated via three osmolyte transporters including OpuC, carnitine uptake for cryoprotective purposes, OpuB shows no significant contribution to listeral chill tolerance
additional information
-
functional re-association of a substrate-binding protein-dependent ABC-transporter starting from the isolated subunits
additional information
Na+-betaine symporter that contributes to the salt stress tolerance at alkaline pH
additional information
-
osmotic control of the OpuA operon allows the cell to sensitively adjust the number of the OpuA transporter to the physiological need of the cell
additional information
the cystathionine beta-synthase module in OpuA constitutes the ionic strength sensor whose activity is modulated by the C-terminal anionic tail
additional information
-
the cystathionine beta-synthase module in OpuA constitutes the ionic strength sensor whose activity is modulated by the C-terminal anionic tail
additional information
-
the cystathionine beta-synthase module in OpuA constitutes the ionic strength sensor whose activity is modulated by the C-terminal anionic tail
-
additional information
-
betaine and carnitine transport upon low temperature exposure is mediated via three osmolyte transporters including OpuC, carnitine uptake for cryoprotective purposes, OpuB shows no significant contribution to listeral chill tolerance
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barron, A.; Jung, J.U.; Villarejo, M.
Purification and characterization of a glycine betaine binding protein from Escherichia coli
J. Biol. Chem.
262
11841-11846
1987
Escherichia coli
brenda
Van der Heide, T.; Poolman, B.
Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane
Proc. Natl. Acad. Sci. USA
97
7102-7106
2000
Bacillus subtilis, Lactococcus lactis, Lactococcus lactis OpuA
brenda
May, G.; Faatz, E.; Villarejo, M.; Bremer, E.
Binding protein dependent transport of glycine betaine and its osmotic regulation in Escherichia coli K12
Mol. Gen. Genet.
205
225-233
1986
Escherichia coli
brenda
Kempf, B.; Bremer, E.
OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis
J. Biol. Chem.
270
16701-16713
1995
Bacillus subtilis, Bacillus subtilis OpuA
brenda
Kempf, B.; Gade, J.; Bremer, E.
Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant
J. Bacteriol.
179
6213-6220
1997
Bacillus subtilis
brenda
Obis, D.; Guillot, A.; Gripon, J.C.; Renault, P.; Bolotin, A.; Mistou, M.Y.
Genetic and biochemical characterization of a high-affinity betaine uptake system (BusA) in Lactococcus lactis reveals a new functional organization within bacterial ABC transporters
J. Bacteriol.
181
6238-6246
1999
Lactococcus lactis, Lactococcus lactis OpuA
brenda
Gerhardt, P.N.; Tombras Smith, L.; Smith, G.M.
Osmotic and chill activation of glycine betaine porter II in Listeria monocytogenes membrane vesicles
J. Bacteriol.
182
2544-2550
2000
Listeria monocytogenes
brenda
Ko, R.; Smith, L.T.
Identification of an ATP-driven, osmoregulated glycine betaine transport system in Listeria monocytogenes
Appl. Environ. Microbiol.
65
4040-4048
1999
Listeria monocytogenes
brenda
Kappes, R.M.; Kempf, B.; Bremer, E.
Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD
J. Bacteriol.
178
5071-5079
1996
Bacillus subtilis
brenda
van der Heide, T.; Stuart, M.C.A.; Poolman, B.
On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine
EMBO J.
20
7022-7032
2001
Lactococcus lactis
brenda
Biemans-Oldehinkel, E.; Poolman, B.
On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA
EMBO J.
22
5983-5993
2003
Lactococcus lactis, Lactococcus lactis NZ9000
brenda
Horn, C.; Bremer, E.; Schmitt, L.
Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis
J. Mol. Biol.
334
403-419
2003
Bacillus subtilis
brenda
Patzlaff, J.S.; van der Heide, T.; Poolman, B.
The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
J. Biol. Chem.
278
29546-29551
2003
Lactococcus lactis, Lactococcus lactis NZ9000
brenda
Romeo, Y.; Obis, D.; Bouvier, J.; Guillot, A.; Fourans, A.; Bouvier, I.; Gutierrez, C.; Mistou, MY.
Osmoregulation in Lactococcus lactis: BusR, a transcriptional repressor of the glycine betaine uptake system BusA
Mol. Microbiol.
47
1135-1147
2003
Lactococcus lactis
brenda
Wemekamp-Kamphuis, H.H.; Sleator, R.D.; Wouters, J.A.; Hill, C.; Abee, T.
Molecular and physiological analysis of the role of osmolyte transporters BetL, Gbu, and OpuC in growth of Listeria monocytogenes at low temperatures
Appl. Environ. Microbiol.
70
2912-2918
2004
Listeria monocytogenes, Listeria monocytogenes LO28
brenda
Laloknam, S.; Tanaka, K.; Buaboocha, T.; Waditee, R.; Incharoensakdi, A.; Hibino, T.; Tanaka, Y.; Takabe, T.
Halotolerant cyanobacterium Aphanothece halophytica contains a betaine transporter active at alkaline pH and high salinity
Appl. Environ. Microbiol.
72
6018-6026
2006
Aphanothece halophytica (Q0PCR9)
brenda
Horn, C.; Bremer, E.; Schmitt, L.
Functional overexpression and in vitro re-association of OpuA, an osmotically regulated ABC-transport complex from Bacillus subtilis
FEBS Lett.
579
5765-5768
2005
Bacillus subtilis
brenda
Holtmann, G.; Bremer, E.
Thermoprotection of Bacillus subtilis by exogenously provided glycine betaine and structurally related compatible solutes: involvement of Opu transporters
J. Bacteriol.
186
1683-1693
2004
Bacillus subtilis
brenda
Cetin, M.S.; Zhang, C.; Hutkins, R.W.; Benson, A.K.
Regulation of transcription of compatible solute transporters by the general stress sigma factor, sigmaB, in Listeria monocytogenes
J. Bacteriol.
186
794-802
2004
Listeria monocytogenes, Listeria monocytogenes 10403S
brenda
Mahmood, N.A.; Biemans-Oldehinkel, E.; Patzlaff, J.S.; Schuurman-Wolters, G.K.; Poolman, B.
Ion specificity and ionic strength dependence of the osmoregulatory ABC transporter OpuA
J. Biol. Chem.
281
29830-29839
2006
Lactococcus lactis (Q9KIF7), Lactococcus lactis, Lactococcus lactis IL1403 (Q9KIF7)
brenda
Horn, C.; Sohn-Boesser, L.; Breed, J.; Welte, W.; Schmitt, L.; Bremer, E.
Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine
J. Mol. Biol.
357
592-606
2006
Bacillus subtilis
brenda
Horn, C.; Jenewein, S.; Sohn-Boesser, L.; Bremer, E.; Schmitt, L.
Biochemical and structural analysis of the Bacillus subtilis ABC transporter OpuA and its isolated subunits
J. Mol. Microbiol. Biotechnol.
10
76-91
2005
Bacillus subtilis, Lactococcus lactis
brenda
Chen, C.; Beattie, G.A.
Characterization of the osmoprotectant transporter OpuC from Pseudomonas syringae and demonstration that cystathionine-beta-synthase domains are required for its osmoregulatory function
J. Bacteriol.
189
6901-6912
2007
Pseudomonas syringae (Q87WH5)
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
Bacillus subtilis (P46920), Bacillus subtilis
brenda
Dreux, N.; Albagnac, C.; Sleator, R.D.; Hill, C.; Carlin, F.; Morris, C.E.; Nguyen-the, C.
Glycine betaine improves Listeria monocytogenes tolerance to desiccation on parsley leaves independent of the osmolyte transporters BetL, Gbu and OpuC
J. Appl. Microbiol.
104
1221-1227
2008
Listeria monocytogenes, Listeria monocytogenes LO28
brenda
Smits, S.H.; Hoeing, M.; Lecher, J.; Jebbar, M.; Schmitt, L.; Bremer, E.
The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies
J. Bacteriol.
190
5663-5671
2008
Bacillus subtilis (P46922), Bacillus subtilis
brenda
Du, Y.; Shi, W.W.; He, Y.X.; Yang, Y.H.; Zhou, C.Z.; Chen, Y.
Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC
Biochem. J.
436
283-289
2011
Bacillus subtilis (O32243), Bacillus subtilis
brenda
Gul, N.; Schuurman-Wolters, G.; Karasawa, A.; Poolman, B.
Functional characterization of amphipathic alpha-helix in the osmoregulatory ABC transporter OpuA
Biochemistry
51
5142-5152
2012
Lactococcus lactis
brenda
Pittelkow, M.; Tschapek, B.; Smits, S.H.; Schmitt, L.; Bremer, E.
The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline
J. Mol. Biol.
411
53-67
2011
Bacillus subtilis (Q45462), Bacillus subtilis, Bacillus subtilis JH642 (Q45462)
brenda
Pilonieta, M.C.; Nagy, T.A.; Jorgensen, D.R.; Detweiler, C.S.
A glycine betaine importer limits Salmonella stress resistance and tissue colonization by reducing trehalose production
Mol. Microbiol.
84
296-309
2012
Salmonella enterica
brenda
Wolters, J.; Ronnie, P.; Gul, N.; Karasawa, A.; Andy-Mark, W.; Slotboom, D.; Poolman, B.
Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA
PLoS ONE
5
e10361
2010
Lactococcus lactis (Q7DAU8), Lactococcus lactis
brenda
Hoffmann, T.; Wensing, A.; Brosius, M.; Steil, L.; Voelker, U.; Bremer, E.
Osmotic control of opuA expression in Bacillus subtilis and its modulation in response to intracellular glycine betaine and proline pools
J. Bacteriol.
195
510-522
2013
Bacillus subtilis, Bacillus subtilis JH642
brenda
Karasawa, A.; Swier, L.J.; Stuart, M.C.; Brouwers, J.; Helms, B.; Poolman, B.
Physicochemical factors controlling the activity and energy coupling of an ionic strength-gated ATP-binding cassette (ABC) transporter
J. Biol. Chem.
288
29862-29871
2013
Lactococcus lactis, Lactococcus lactis Opu401
brenda
Bashir, A.; Hoffmann, T.; Kempf, B.; Xie, X.; Smits, S.; Bremer, E.
Plant-derived compatible solutes proline betaine and betonicine confer enhanced osmotic and temperature stress tolerance to Bacillus subtilis
Microbiology
160
2283-2294
2014
Bacillus subtilis
brenda
Gul, N.; Poolman, B.
Functional reconstitution and osmoregulatory properties of the ProU ABC transporter from Escherichia coli
Mol. Membr. Biol.
30
138-148
2013
Escherichia coli
brenda
Teichmann, L.; Kuemmel, H.; Warmbold, B.; Bremer, E.
OpuF a new Bacillus compatible solute ABC transporter with a substrate-binding protein fused to the trans-membrane domain
Appl. Environ. Microbiol.
84
e01728-18
2018
no activity in Bacillus subtilis, Bacillus infantis, Ectobacillus panaciterrae
brenda
Ronzheimer, S.; Warmbold, B.; Arnhold, C.; Bremer, E.
The GbsR family of transcriptional regulators functional characterization of the OpuAR repressor
Front. Microbiol.
9
2536
2018
Bacillus subtilis (P46921), Bacillus subtilis (P46922), Bacillus infantis (U5LFB4 AND U5LHK3 AND U5LHN4), Bacillus subtilis 168 (P46921), Bacillus subtilis 168 (P46922), Bacillus infantis NRRL B-14911 (U5LFB4 AND U5LHK3 AND U5LHN4)
brenda
Ma, Y.; Wang, Q.; Gao, X.; Zhang, Y.
Biosynthesis and uptake of glycine betaine as cold-stress response to low temperature in fish pathogen Vibrio anguillarum
J. Microbiol.
55
44-55
2017
Vibrio anguillarum serotype O1 (A0A077T980 AND A0A077T7U5 AND A0A077T7Z1), Vibrio anguillarum serotype O1 (A0A097A5F2 AND A0A077T7R8), Vibrio anguillarum serotype O1 MVM425 (A0A077T980 AND A0A077T7U5 AND A0A077T7Z1), Vibrio anguillarum serotype O1 MVM425 (A0A097A5F2 AND A0A077T7R8)
brenda
Teichmann, L.; Chen, C.; Hoffmann, T.; Smits, S.H.J.; Schmitt, L.; Bremer, E.
From substrate specificity to promiscuity hybrid ABC transporters for osmoprotectants
Mol. Microbiol.
104
761-780
2017
Bacillus subtilis (P46921), Bacillus subtilis (P46922), Bacillus subtilis, Bacillus subtilis 168 (P46921), Bacillus subtilis 168 (P46922), Bacillus subtilis JH642 (P46921), Bacillus subtilis JH642 (P46922)
brenda
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EXTERNAL LINKS (specific for EC-Number 7.6.2.9)
Transporter Classification Database (TCDB): 3.A.1.12.2
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