7.6.2.9: ABC-type quaternary amine transporter
This is an abbreviated version!
For detailed information about ABC-type quaternary amine transporter, go to the full flat file.
Word Map on EC 7.6.2.9
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7.6.2.9
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cassette
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multidrug
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p-glycoprotein
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nucleotide-binding
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toxin
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streptococcus
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lipoprotein
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xenobiotics
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bacteriocins
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azole
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doxorubicin
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verapamil
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siderophore
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cftr
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resistance-associated
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chemoresistance
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lactococcus
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two-component
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hoechst
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cystic
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rhodamine
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elasticum
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atp-bound
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nisin
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mitoxantrone
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molecular biology
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cry1ac
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abc-transporter
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abcb11
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azole-resistant
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calcein
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ivermectin
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proteoliposomes
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atp-driven
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lantibiotic
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abcg2-mediated
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pseudoxanthoma
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flippase
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abccs
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transporter-mediated
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thuringiensis
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triphosphate-binding
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outward-facing
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canalicular
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stargardt
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bacitracin
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adrenoleukodystrophy
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fluconazole
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nucleotide-free
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itraconazole
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inward-facing
- 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
Reaction
Synonyms
ABC transporter, BetTA.halophytica, EC 3.6.3.32, glycine betaine porter II, glycine betaine transport system permease protein, glycine betaine transporter membrane protein, glycine betaine-binding protein, glycine betaine-binding protein OpuAC, glycine betaine/carnitine/choline-binding protein, glycine/betaine ABC transporter, N288_21505, N288_21525, N288_25665, OpuA, OpuAB, OpuAC, OpuB, OpuBC, OpuC, OpuCC, OpuD, OpuF, OpuF transporter, proline/betaine ABC transporter permease, ProU, proW, Quaternary-amine-transporting ATPase
ECTree
7.6.2.9 ABC-type quaternary amine transporterAdvanced search results
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results (Engineering
Engineering on EC 7.6.2.9 - ABC-type quaternary amine transporter
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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
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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. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
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
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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. OpuC transporter lacking its solute receptor protein OpuBC is nonfunctional, which is also true for OpuB
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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
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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. 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
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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
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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
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mutants LO28deltaB, LO28deltaC, LO28deltaG, LO28deltaBG, LO28deltaCG, LO28deltaBCG, LO28deltaBCGsoe, LO28deltaBCGB, deletion of osmolyte transporters reduces growth at low temperatures
additional information
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mutants LO28deltaB, LO28deltaC, LO28deltaG, LO28deltaBG, LO28deltaCG, LO28deltaBCG, LO28deltaBCGsoe, LO28deltaBCGB, deletion of osmolyte transporters reduces growth at low temperatures
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additional information
deletion mutants of OpuC generated, complementation of deletion mutants shown
