EC Number   |
General Information |
Reference |
|---|
   7.6.2.9 | 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 |
749673 |
| 7.6.2.9 | 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 |
749673 |
| 7.6.2.9 | 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) |
-, 750650 |
| 7.6.2.9 | 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 |
-, 750650 |
| 7.6.2.9 | 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) |
-, 750650 |
| 7.6.2.9 | 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 |
-, 751583 |
| 7.6.2.9 | malfunction |
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 |
-, 751296 |
| 7.6.2.9 | malfunction |
OpuB transporter lacking its solute receptor protein OpuBC is nonfunctional |
-, 751583 |
| 7.6.2.9 | malfunction |
OpuC transporter lacking its solute receptor protein OpuCC is nonfunctional |
-, 751583 |
| 7.6.2.9 | more |
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 |
749673 |
