| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALP40305.1 | ALP40433.1 | WL1483_886 | WL1483_1014 | Peptide ABC transporter permease. | ABC transporter permease. | 0.809 |
| ALP40305.1 | lolD | WL1483_886 | WL1483_1894 | Peptide 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. | 0.844 |
| ALP40305.1 | macB2 | WL1483_886 | WL1483_1440 | Peptide ABC transporter permease. | Macrolide-specific ABC-type efflux carrier; 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. | 0.801 |
| ALP40433.1 | ALP40305.1 | WL1483_1014 | WL1483_886 | ABC transporter permease. | Peptide ABC transporter permease. | 0.809 |
| ALP40433.1 | lolD | WL1483_1014 | WL1483_1894 | 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. | 0.911 |
| ALP40433.1 | macB2 | WL1483_1014 | WL1483_1440 | ABC transporter permease. | Macrolide-specific ABC-type efflux carrier; 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. | 0.802 |
| ALP42171.1 | lolA | WL1483_2752 | WL1483_1051 | Hypothetical protein. | Outer membrane lipoprotein carrier protein LolA; 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). | 0.798 |
| ALP42171.1 | lolD | WL1483_2752 | WL1483_1894 | Hypothetical 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. | 0.839 |
| ALP42171.1 | macB2 | WL1483_2752 | WL1483_1440 | Hypothetical protein. | Macrolide-specific ABC-type efflux carrier; 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. | 0.895 |
| ALP43186.1 | lolA | WL1483_3767 | WL1483_1051 | Antimicrobial peptide ABC transporter permease. | Outer membrane lipoprotein carrier protein LolA; 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). | 0.667 |
| ALP43186.1 | lolD | WL1483_3767 | WL1483_1894 | Antimicrobial peptide 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. | 0.808 |
| ALP43186.1 | macB2 | WL1483_3767 | WL1483_1440 | Antimicrobial peptide ABC transporter permease. | Macrolide-specific ABC-type efflux carrier; 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. | 0.895 |
| lolA | ALP42171.1 | WL1483_1051 | WL1483_2752 | Outer membrane lipoprotein carrier protein LolA; 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). | Hypothetical protein. | 0.798 |
| lolA | ALP43186.1 | WL1483_1051 | WL1483_3767 | Outer membrane lipoprotein carrier protein LolA; 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). | Antimicrobial peptide ABC transporter permease. | 0.667 |
| lolA | lolC | WL1483_1051 | WL1483_1291 | Outer membrane lipoprotein carrier protein LolA; 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). | Transporter. | 0.875 |
| lolA | lolD | WL1483_1051 | WL1483_1894 | Outer membrane lipoprotein carrier protein LolA; 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). | Lipoprotein releasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.829 |
| lolA | lolE | WL1483_1051 | WL1483_1962 | Outer membrane lipoprotein carrier protein LolA; 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). | Lipoprotein releasing system, transmembrane protein LolE. | 0.873 |
| lolA | macB2 | WL1483_1051 | WL1483_1440 | Outer membrane lipoprotein carrier protein LolA; 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). | Macrolide-specific ABC-type efflux carrier; 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. | 0.745 |
| lolC | lolA | WL1483_1291 | WL1483_1051 | Transporter. | Outer membrane lipoprotein carrier protein LolA; 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). | 0.875 |
| lolC | lolD | WL1483_1291 | WL1483_1894 | Transporter. | Lipoprotein releasing system, ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.992 |