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Literature summary for 7.6.2.9 extracted from
- From substrate specificity to promiscuity hybrid ABC transporters for osmoprotectants (2017), Mol. Microbiol., 104, 761-780 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 | Bacillus subtilis |
| 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 | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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 | Bacillus subtilis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Bacillus subtilis | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Bacillus subtilis |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] | Bacillus subtilis | - |
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] | - |
? | |
| ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] | Bacillus subtilis 168 | - |
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] | - |
? | |
| ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] | Bacillus subtilis JH642 | - |
ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P46921 | glycine betaine transport system permease protein OpuAB | - |
| Bacillus subtilis | P46922 | glycine betaine-binding protein OpuAC | - |
| Bacillus subtilis 168 | P46921 | glycine betaine transport system permease protein OpuAB | - |
| Bacillus subtilis 168 | P46922 | glycine betaine-binding protein OpuAC | - |
| Bacillus subtilis JH642 | P46921 | glycine betaine transport system permease protein OpuAB | - |
| Bacillus subtilis JH642 | P46922 | glycine betaine-binding protein OpuAC | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] | - |
Bacillus subtilis | ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] | - |
? | |
| ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] | - |
Bacillus subtilis 168 | ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] | - |
? | |
| ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] | - |
Bacillus subtilis JH642 | ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | 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 | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glycine betaine transport system permease protein | - |
Bacillus subtilis |
| glycine betaine-binding protein | - |
Bacillus subtilis |
| OpuAB | - |
Bacillus subtilis |
| OpuAC | - |
Bacillus subtilis |
| OpuB | - |
Bacillus subtilis |
| OpuC | - |
Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Bacillus subtilis | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Bacillus subtilis | the trans-acting regulatory gene gbsR encodes a repressor (GbsR) for the opuB operon | down |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Bacillus subtilis |
| malfunction | OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional | Bacillus subtilis |
| malfunction | OpuC transporter lacking its solute receptor protein OpuCC is nonfunctional | Bacillus subtilis |
| 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 | Bacillus subtilis |
| 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 | Bacillus subtilis |
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