node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ95198.1 | CAZ95200.1 | ZOBELLIA_1141 | ZOBELLIA_1143 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | 0.996 |
CAZ95198.1 | CAZ95567.1 | ZOBELLIA_1141 | ZOBELLIA_1511 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.930 |
CAZ95198.1 | CAZ95569.1 | ZOBELLIA_1141 | ZOBELLIA_1513 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide of lipoprotein cleaved between the residues 21 and 22; Localized in the outer membrane; Family membership. | 0.900 |
CAZ95198.1 | CAZ95998.1 | ZOBELLIA_1141 | ZOBELLIA_1945 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.939 |
CAZ95198.1 | CAZ95999.1 | ZOBELLIA_1141 | ZOBELLIA_1946 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | 0.917 |
CAZ95198.1 | CAZ96548.1 | ZOBELLIA_1141 | ZOBELLIA_2395 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; belongs to the type I secretion system; Family membership. | 0.431 |
CAZ95198.1 | CAZ96549.1 | ZOBELLIA_1141 | ZOBELLIA_2396 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | 0.908 |
CAZ95198.1 | CAZ97064.1 | ZOBELLIA_1141 | ZOBELLIA_2917 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; Belongs to the type I secretion system; Family membership. | 0.930 |
CAZ95198.1 | CAZ97066.1 | ZOBELLIA_1141 | ZOBELLIA_2919 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Lipoprotein-type signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Family membership. | 0.900 |
CAZ95198.1 | CAZ98409.1 | ZOBELLIA_1141 | ZOBELLIA_4274 | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria; Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Belongs to the type I secretion system; Family membership. | 0.900 |
CAZ95200.1 | CAZ95198.1 | ZOBELLIA_1143 | ZOBELLIA_1141 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | 0.996 |
CAZ95200.1 | CAZ95567.1 | ZOBELLIA_1143 | ZOBELLIA_1511 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.900 |
CAZ95200.1 | CAZ95569.1 | ZOBELLIA_1143 | ZOBELLIA_1513 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide of lipoprotein cleaved between the residues 21 and 22; Localized in the outer membrane; Family membership. | 0.866 |
CAZ95200.1 | CAZ95998.1 | ZOBELLIA_1143 | ZOBELLIA_1945 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | 0.900 |
CAZ95200.1 | CAZ95999.1 | ZOBELLIA_1143 | ZOBELLIA_1946 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 19 and 20; Localized in the outer membrane; Family membership. | 0.930 |
CAZ95200.1 | CAZ96549.1 | ZOBELLIA_1143 | ZOBELLIA_2396 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | 0.930 |
CAZ95200.1 | CAZ97064.1 | ZOBELLIA_1143 | ZOBELLIA_2917 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; Belongs to the type I secretion system; Family membership. | 0.900 |
CAZ95200.1 | CAZ97066.1 | ZOBELLIA_1143 | ZOBELLIA_2919 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Lipoprotein-type signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Family membership. | 0.866 |
CAZ95200.1 | CAZ98409.1 | ZOBELLIA_1143 | ZOBELLIA_4274 | The membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmic membrane by a N-terminal transmembrane region; participates to the type I secretion system; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria; Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Belongs to the type I secretion system; Family membership. | 0.930 |
CAZ95567.1 | CAZ95198.1 | ZOBELLIA_1511 | ZOBELLIA_1141 | These membrane fusion proteins (MFP) belong to a multidrug efflux pump system that confer the resistance to compounds such as antibiotics, solvents or heavy metals; Proteins of the MFP family function as 'adaptors', connecting a ABC transporters, localized in the cytoplasmic membrane, with a porin or channel localized in outer membrane; The MFP proteins seem to be anchored in the cytoplasmique membrane by a N-terminal transmembrane region; Family membership. | The outer membrane efflux proteins (OEP) are composed of two repeats of OEP domain to form a trimeric channel continuous, solvent-accessible conduit that spans both the outer membrane and periplasmic space; May be specialized for the signal peptide independent extracellular secretion of a variety of substrates in Gram-negative bacteria (type I secretion system); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | 0.930 |