| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALU99444.1 | creD | ATE51_01842 | ATE51_01836 | Lipoprotein chaperone; 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). | Inner membrane protein CreD. | 0.541 |
| ALU99444.1 | ftsE | ATE51_01842 | ATE51_02424 | Lipoprotein chaperone; 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). | Cell division ATP-binding protein FtsE. | 0.471 |
| ALU99444.1 | lolD_1 | ATE51_01842 | ATE51_00194 | Lipoprotein chaperone; 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 LolD. | 0.471 |
| ALU99444.1 | lolD_2 | ATE51_01842 | ATE51_01246 | Lipoprotein chaperone; 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 LolD. | 0.471 |
| ALU99444.1 | lolE | ATE51_01842 | ATE51_01838 | Lipoprotein chaperone; 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. | 0.801 |
| ALU99444.1 | macB_3 | ATE51_01842 | ATE51_02374 | Lipoprotein chaperone; 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 export ATP-binding/permease protein MacB; Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.678 |
| ALU99444.1 | pal | ATE51_01842 | ATE51_04238 | Lipoprotein chaperone; 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). | Peptidoglycan-associated lipoprotein precursor; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 0.408 |
| ALU99444.1 | secA | ATE51_01842 | ATE51_01840 | Lipoprotein chaperone; 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). | Preprotein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. | 0.676 |
| bamA | lolE | ATE51_04204 | ATE51_01838 | Outer membrane protein assembly factor BamA precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Lipoprotein-releasing system transmembrane protein LolE. | 0.793 |
| bamA | pal | ATE51_04204 | ATE51_04238 | Outer membrane protein assembly factor BamA precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Peptidoglycan-associated lipoprotein precursor; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 0.854 |
| bamA | secA | ATE51_04204 | ATE51_01840 | Outer membrane protein assembly factor BamA precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Preprotein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. | 0.708 |
| creD | ALU99444.1 | ATE51_01836 | ATE51_01842 | Inner membrane protein CreD. | Lipoprotein chaperone; 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). | 0.541 |
| creD | lolE | ATE51_01836 | ATE51_01838 | Inner membrane protein CreD. | Lipoprotein-releasing system transmembrane protein LolE. | 0.776 |
| creD | secA | ATE51_01836 | ATE51_01840 | Inner membrane protein CreD. | Preprotein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family. | 0.773 |
| ftsE | ALU99444.1 | ATE51_02424 | ATE51_01842 | Cell division ATP-binding protein FtsE. | Lipoprotein chaperone; 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). | 0.471 |
| ftsE | lolE | ATE51_02424 | ATE51_01838 | Cell division ATP-binding protein FtsE. | Lipoprotein-releasing system transmembrane protein LolE. | 0.603 |
| ftsE | macB_3 | ATE51_02424 | ATE51_02374 | Cell division ATP-binding protein FtsE. | Macrolide export ATP-binding/permease protein MacB; Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.619 |
| lolD_1 | ALU99444.1 | ATE51_00194 | ATE51_01842 | Lipoprotein-releasing system ATP-binding protein LolD. | Lipoprotein chaperone; 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). | 0.471 |
| lolD_1 | lolE | ATE51_00194 | ATE51_01838 | Lipoprotein-releasing system ATP-binding protein LolD. | Lipoprotein-releasing system transmembrane protein LolE. | 0.603 |
| lolD_1 | macB_3 | ATE51_00194 | ATE51_02374 | Lipoprotein-releasing system ATP-binding protein LolD. | Macrolide export ATP-binding/permease protein MacB; Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. | 0.619 |
