| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ggt | coaD | Lche_0460 | Lche_0459 | Gamma-glutamyltranspeptidase. | Pantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.839 |
| Ggt | lolB | Lche_0460 | Lche_0458 | Gamma-glutamyltranspeptidase. | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.747 |
| bamD | lolA | Lche_1887 | Lche_1366 | Competence lipoprotein comL precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Outer-membrane lipoprotein carrier protein precursor; 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). | 0.700 |
| bamD | lolB | Lche_1887 | Lche_0458 | Competence lipoprotein comL precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.793 |
| bamD | lolCE | Lche_1887 | Lche_0227 | Competence lipoprotein comL 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 LolC/E. | 0.605 |
| bamD | minE | Lche_1887 | Lche_1417 | Competence lipoprotein comL precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | Septum formation topological specificity factor; Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | 0.609 |
| coaD | Ggt | Lche_0459 | Lche_0460 | Pantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Gamma-glutamyltranspeptidase. | 0.839 |
| coaD | lolB | Lche_0459 | Lche_0458 | Pantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.747 |
| ftsL | lolB | Lche_1010 | Lche_0458 | Cell division transmembrane protein FtsL; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.757 |
| hemY | lolB | Lche_0008 | Lche_0458 | Protoporphyrinogen oxidase. | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.770 |
| lolA | bamD | Lche_1366 | Lche_1887 | Outer-membrane lipoprotein carrier protein precursor; 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). | Competence lipoprotein comL precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.700 |
| lolA | lolB | Lche_1366 | Lche_0458 | Outer-membrane lipoprotein carrier protein precursor; 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). | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.965 |
| lolA | lolCE | Lche_1366 | Lche_0227 | Outer-membrane lipoprotein carrier protein precursor; 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 LolC/E. | 0.967 |
| lolA | lolD | Lche_1366 | Lche_0226 | Outer-membrane lipoprotein carrier protein precursor; 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. | 0.945 |
| lolB | Ggt | Lche_0458 | Lche_0460 | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Gamma-glutamyltranspeptidase. | 0.747 |
| lolB | bamD | Lche_0458 | Lche_1887 | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Competence lipoprotein comL precursor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.793 |
| lolB | coaD | Lche_0458 | Lche_0459 | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Pantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. | 0.747 |
| lolB | ftsL | Lche_0458 | Lche_1010 | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Cell division transmembrane protein FtsL; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | 0.757 |
| lolB | hemY | Lche_0458 | Lche_0008 | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Protoporphyrinogen oxidase. | 0.770 |
| lolB | lolA | Lche_0458 | Lche_1366 | Molecular chaperone LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | Outer-membrane lipoprotein carrier protein precursor; 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). | 0.965 |
