| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABK72746.1 | mspA | MSMEG_1528 | MSMEG_0965 | Cutinase; Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | 0.507 |
| ABK73124.1 | mspA | MSMEG_0194 | MSMEG_0965 | Serine esterase, cutinase family protein; Identified by match to protein family HMM PF01083. | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | 0.507 |
| lfrA | mspA | MSMEG_6225 | MSMEG_0965 | Proton antiporter efflux pump; Energy-dependent efflux pump that contributes to drug resistance. Catalyzes the efflux of norfloxacin and several related fluoroquinolones (FQ). Contributes significantly to the intrinsic MICs for ethidium bromide and acriflavine. Overexpression confers low-level resistance to hydrophilic FQ such as ciprofloxacin, ofloxacin and levofloxacin, and to ethidium bromide, acridine, acriflavine, rhodamine 123 and some quaternary ammonium compounds. May contribute to resistance to certain beta-lactams. Probably uses the proton motive force. | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | 0.425 |
| mscL | mspA | MSMEG_5482 | MSMEG_0965 | Large conductance mechanosensitive channel protein; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | 0.402 |
| mspA | ABK72746.1 | MSMEG_0965 | MSMEG_1528 | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | Cutinase; Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. | 0.507 |
| mspA | ABK73124.1 | MSMEG_0965 | MSMEG_0194 | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | Serine esterase, cutinase family protein; Identified by match to protein family HMM PF01083. | 0.507 |
| mspA | lfrA | MSMEG_0965 | MSMEG_6225 | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | Proton antiporter efflux pump; Energy-dependent efflux pump that contributes to drug resistance. Catalyzes the efflux of norfloxacin and several related fluoroquinolones (FQ). Contributes significantly to the intrinsic MICs for ethidium bromide and acriflavine. Overexpression confers low-level resistance to hydrophilic FQ such as ciprofloxacin, ofloxacin and levofloxacin, and to ethidium bromide, acridine, acriflavine, rhodamine 123 and some quaternary ammonium compounds. May contribute to resistance to certain beta-lactams. Probably uses the proton motive force. | 0.425 |
| mspA | mscL | MSMEG_0965 | MSMEG_5482 | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] | Large conductance mechanosensitive channel protein; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell. | 0.402 |
