| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CED57445.1 | lolA | AWOD_II_0820 | AWOD_I_0888 | ABC transporter, permease component. | Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.678 |
| CED57445.1 | lolD | AWOD_II_0820 | AWOD_II_0531 | ABC transporter, permease component. | Lipoprotein-releasing system ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.728 |
| CED57445.1 | macB | AWOD_II_0820 | AWOD_II_1146 | ABC transporter, permease component. | ABC transporter, permease; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.797 |
| CED70957.1 | lolA | AWOD_I_0864 | AWOD_I_0888 | Predicted permease. | Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.678 |
| CED70957.1 | lolD | AWOD_I_0864 | AWOD_II_0531 | Predicted permease. | Lipoprotein-releasing system ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.678 |
| CED70957.1 | macB | AWOD_I_0864 | AWOD_II_1146 | Predicted permease. | ABC transporter, permease; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.797 |
| CED71186.1 | CED71187.1 | AWOD_I_1100 | AWOD_I_1101 | Putative ABC transporter permease. | Putative ABC transporter permease. | 0.845 |
| CED71186.1 | lolA | AWOD_I_1100 | AWOD_I_0888 | Putative ABC transporter permease. | Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.678 |
| CED71186.1 | lolD | AWOD_I_1100 | AWOD_II_0531 | Putative ABC transporter permease. | Lipoprotein-releasing system ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.743 |
| CED71186.1 | macB | AWOD_I_1100 | AWOD_II_1146 | Putative ABC transporter permease. | ABC transporter, permease; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.797 |
| CED71187.1 | CED71186.1 | AWOD_I_1101 | AWOD_I_1100 | Putative ABC transporter permease. | Putative ABC transporter permease. | 0.845 |
| CED71187.1 | lolA | AWOD_I_1101 | AWOD_I_0888 | Putative ABC transporter permease. | Outer-membrane lipoprotein carrier protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.678 |
| CED71187.1 | lolD | AWOD_I_1101 | AWOD_II_0531 | Putative ABC transporter permease. | Lipoprotein-releasing system ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.748 |
| CED71187.1 | lolE | AWOD_I_1101 | AWOD_II_0532 | Putative ABC transporter permease. | Lipoprotein-releasing system transmembrane protein. | 0.423 |
| CED71187.1 | macB | AWOD_I_1101 | AWOD_II_1146 | Putative ABC transporter permease. | ABC transporter, permease; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.797 |
| CED71237.1 | CED71238.1 | AWOD_I_1152 | AWOD_I_1153 | ABC transporter, permease protein. | ABC transporter, permease protein. | 0.864 |
| CED71237.1 | lolD | AWOD_I_1152 | AWOD_II_0531 | ABC transporter, permease protein. | Lipoprotein-releasing system ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.820 |
| CED71237.1 | macB | AWOD_I_1152 | AWOD_II_1146 | ABC transporter, permease protein. | ABC transporter, permease; Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.728 |
| CED71238.1 | CED71237.1 | AWOD_I_1153 | AWOD_I_1152 | ABC transporter, permease protein. | ABC transporter, permease protein. | 0.864 |
| CED71238.1 | lolD | AWOD_I_1153 | AWOD_II_0531 | ABC transporter, permease protein. | Lipoprotein-releasing system ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.751 |