Cloned (Comment) | Organism |
---|---|
expression in Lactococcus lactis | Lactococcus lactis |
Protein Variants | Comment | Organism |
---|---|---|
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 | Lactococcus lactis |
S24C | 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 | Lactococcus lactis |
T23C | 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 | Lactococcus lactis |
T25C | 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 | Lactococcus lactis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | 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 | Lactococcus lactis | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lactococcus lactis | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
OpuA | - |
Lactococcus lactis |
General Information | Comment | Organism |
---|---|---|
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 | Lactococcus lactis |