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ATP + H2O
ADP + phosphate
ADP + H2O
AMP + phosphate
-
OpuAA protein, ATPase activity
-
-
?
AMP + H2O
adenine + phosphate
-
OpuAA protein, ATPase activity, similar substrate affinities to monomeric and dimeric states
-
-
?
ATP + H2O
ADP + phosphate
ATP + H2O + betaine/out
ADP + phosphate + betaine/in
-
-
-
-
?
ATP + H2O + betonicine/out
ADP + phosphate + betonicine/in
-
-
-
-
?
ATP + H2O + dimethylsulfonioacetate/out
ADP + phosphate + dimethylsulfonioacetate/in
ATP + H2O + glycine betaine/out
ADP + phosphate + glycine betaine/in
ATP + H2O + L-proline betaine/out
ADP + phosphate + L-proline betaine/in
-
-
-
-
?
ATP + H2O + proline betaine/out
ADP + phosphate + 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]
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
?
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
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
OpuAA protein, ATPase activity
-
-
?
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 + 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]
-
-
-
?
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 not a substrate
-
-
?
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ATP + H2O
ADP + phosphate
-
-
-
?
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 + 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]
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 + 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]
-
-
-
?
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0.0024 - 0.013
glycine betaine
additional information
additional information
-
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
0.25
ATP
-
22ºC, pH 8.0, 0.15 M NaCl, monomeric and dimeric OpuAA
0.45
ATP
-
22ºC, pH 8.0, 1 M NaCl, monomeric OpuAA
1.3
ATP
-
22ºC, pH 8.0, 1 M NaCl, dimeric OpuAA
5.4
ATP
-
22ºC, pH 8.0, 1 M KCl, monomeric OpuAA
0.0024
glycine betaine
-
OpuA
0.0051
glycine betaine
-
OpuC, without NaCl
0.006
glycine betaine
-
OpuC, in presence of 0.4 M NaCl
0.0095
glycine betaine
-
OpuD, without NaCl
0.013
glycine betaine
-
OpuD, in presence of 0.4 M NaCl
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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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
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
OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional
malfunction
OpuC transporter lacking its solute receptor protein OpuCC is nonfunctional
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
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
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?
-
x * 56130, calculation from nucleotide sequence
dimer
-
nucleotide-binding protein domain, displays lower ATPase activity than the dimeric form
monomer
-
1 * 65000, gel filtration
monomer
-
nucleotide-binding protein domain, displays higher ATPase activity than the dimeric form
monomer
-
substrate-binding domain, 1 * 28000, SDS-PAGE
additional information
-
-
additional information
-
the transport system consists of an ATPase, OpuAA, an integral membrane protein OpuAB and a hydrophilic polypeptide OpuAC
additional information
-
a peak of 150000 corresponds to dimeric OpuAA
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
-
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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G161C
single cysteine mutants generated by site-directed mutagenesis
S171C
single cysteine mutants generated by site-directed mutagenesis
S45C
single cysteine mutants generated by site-directed mutagenesis
D149A
decrease in choline binding affinity by approximately 18fold
D149A/L155A
decrease in choline binding affinity by approximately 38fold
D74A
mutant is unable to bind choline
E171Q
-
the monomer is the preferred species for the nucleotide-free state in solution
L155A
decrease in choline binding affinity by approximately 25fold
M21A
decrease in choline binding affinity by approximately 3fold
N115A
mutant is unable to bind choline
Q19A
decrease in choline binding affinity by approximately 15fold
Q19A/L155A
mutant is unable to bind choline
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
Y91A
complete loss of binding affinity
Y91F
slight decrease in binding affinity
Y91W
slight decrease in binding affinity
additional information
-
deletion of the various Opu transport systems prevents thermoprotection by compatible solutes
additional information
-
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
-
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
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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
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
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
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
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
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
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
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
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
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
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
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
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