node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
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 | 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 | CAZ97065.1 | ZOBELLIA_1141 | ZOBELLIA_2918 | 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. | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 9 and 10. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | 0.466 |
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 |
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 |
CAZ95567.1 | CAZ95569.1 | ZOBELLIA_1511 | ZOBELLIA_1513 | 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 of lipoprotein cleaved between the residues 21 and 22; Localized in the outer membrane; Family membership. | 0.989 |
CAZ95567.1 | CAZ95998.1 | ZOBELLIA_1511 | ZOBELLIA_1945 | 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. | 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. | 0.914 |
CAZ95567.1 | CAZ95999.1 | ZOBELLIA_1511 | ZOBELLIA_1946 | 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 19 and 20; Localized in the outer membrane; Family membership. | 0.931 |
CAZ95567.1 | CAZ96549.1 | ZOBELLIA_1511 | ZOBELLIA_2396 | 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); Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Family membership. | 0.930 |
CAZ95567.1 | CAZ97064.1 | ZOBELLIA_1511 | ZOBELLIA_2917 | 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. | 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. | 0.918 |
CAZ95567.1 | CAZ97065.1 | ZOBELLIA_1511 | ZOBELLIA_2918 | 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. | Multidrug efflux transporter; Integral membrane protein involved in drug resistance that belongs to the acrB/acrD/acrF family; Contains 12 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 9 and 10. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. | 0.867 |
CAZ95567.1 | CAZ97066.1 | ZOBELLIA_1511 | ZOBELLIA_2919 | 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); Lipoprotein-type signal peptide cleaved between the residues 21 and 22; Localized in the outer membrane; Family membership. | 0.970 |
CAZ95567.1 | CAZ98409.1 | ZOBELLIA_1511 | ZOBELLIA_4274 | 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; Signal peptide cleaved between the residues 18 and 19; Localized in the outer membrane; Belongs to the type I secretion system; Family membership. | 0.940 |
CAZ95567.1 | czcA | ZOBELLIA_1511 | ZOBELLIA_4091 | 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. | Cation efflux transporter; Integral membrane protein possibly involved in cobalt, zinc and cadmium resistance that belongs to the acrB/acrD/acrF family; Contains 13 transmembrane segments and two large periplasmic domains (each exceeding 300 residues) between helices 1 and 2, and helices 7 and 8; Contains a C-terminal extension of 430 residues after the last transmembrane segment. The three transmembrane domains form a large, 30-wide central cavity that spans the cytoplasmic membrane and extends to the cytoplasm; Localized in the cytoplasmic membrane; Family membership; Belongs to the [...] | 0.920 |
CAZ95569.1 | CAZ95198.1 | ZOBELLIA_1513 | ZOBELLIA_1141 | 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. | 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. | 0.900 |