| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| amiB | excC | UGYR_11740 | UGYR_15560 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidoglycan-associated outer membrane lipoprotein; 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. | 0.564 |
| amiB | lolA | UGYR_11740 | UGYR_16435 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.852 |
| amiB | macB | UGYR_11740 | UGYR_16380 | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Macrolide transporter; 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. | 0.562 |
| excC | amiB | UGYR_15560 | UGYR_11740 | Peptidoglycan-associated outer membrane lipoprotein; 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. | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.564 |
| excC | lolA | UGYR_15560 | UGYR_16435 | Peptidoglycan-associated outer membrane lipoprotein; 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. | 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). | 0.891 |
| excC | lolB | UGYR_15560 | UGYR_00790 | Peptidoglycan-associated outer membrane lipoprotein; 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. | Membrane protein; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.841 |
| excC | lolC | UGYR_15560 | UGYR_00365 | Peptidoglycan-associated outer membrane lipoprotein; 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. | Outer membrane-specific lipoprotein transporter subunit LolC; Part of the ATP-dependent transport system LolCDE; responsible for the localization of lipoproteins to the periplasmic surface of the outer membrane; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.811 |
| excC | lolE | UGYR_15560 | UGYR_00375 | Peptidoglycan-associated outer membrane lipoprotein; 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. | Outer membrane-specific lipoprotein transporter subunit LolE; Part of the ATP-dependent transport system LolCDE; responsible for the localization of lipoproteins to the periplasmic surface of the outer membrane; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.806 |
| excC | lpp | UGYR_15560 | UGYR_02320 | Peptidoglycan-associated outer membrane lipoprotein; 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. | Major outer membrane lipoprotein; interacts with peptidoglycan to maintain the integrity of the cell envelope; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.519 |
| excC | macB | UGYR_15560 | UGYR_16380 | Peptidoglycan-associated outer membrane lipoprotein; 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. | Macrolide transporter; 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. | 0.420 |
| ftsK | lolA | UGYR_16430 | UGYR_16435 | Cell division protein FtsK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.861 |
| ftsK | rarA | UGYR_16430 | UGYR_16440 | Cell division protein FtsK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Recombination factor protein RarA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.854 |
| lolA | amiB | UGYR_16435 | UGYR_11740 | 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). | N-acetylmuramoyl-L-alanine amidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
| lolA | excC | UGYR_16435 | UGYR_15560 | 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 outer membrane lipoprotein; 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. | 0.891 |
| lolA | ftsK | UGYR_16435 | UGYR_16430 | 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 protein FtsK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.861 |
| lolA | lolB | UGYR_16435 | UGYR_00790 | 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). | Membrane protein; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. | 0.872 |
| lolA | lolC | UGYR_16435 | UGYR_00365 | 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). | Outer membrane-specific lipoprotein transporter subunit LolC; Part of the ATP-dependent transport system LolCDE; responsible for the localization of lipoproteins to the periplasmic surface of the outer membrane; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.940 |
| lolA | lolD | UGYR_16435 | UGYR_00370 | 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 ABC transporter ATP-binding protein; Part of the ABC transporter complex LolCDE involved in the translocation of lipoproteins, in an ATP-dependent manner. | 0.929 |
| lolA | lolE | UGYR_16435 | UGYR_00375 | 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). | Outer membrane-specific lipoprotein transporter subunit LolE; Part of the ATP-dependent transport system LolCDE; responsible for the localization of lipoproteins to the periplasmic surface of the outer membrane; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.938 |
| lolA | lpp | UGYR_16435 | UGYR_02320 | 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). | Major outer membrane lipoprotein; interacts with peptidoglycan to maintain the integrity of the cell envelope; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.886 |