| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM1254 | lppB | STM1254 | STM1376 | Putative outer membrane lipoprotein. | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | 0.511 |
| STM3216 | lppB | STM3216 | STM1376 | Similar to E. coli methyl-accepting chemotaxis protein I, serine sensor receptor (AAC77311.1); Blastp hit to AAC77311.1 (551 aa), 36% identity in aa 2 - 523. | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | 0.699 |
| lolA | lpp | STM0961 | STM1377 | Periplasmic 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). | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | 0.773 |
| lolA | lppB | STM0961 | STM1376 | Periplasmic 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). | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | 0.603 |
| lolA | msbB | STM0961 | STM1889 | Periplasmic 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). | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | 0.690 |
| lolA | ompA | STM0961 | STM1070 | Periplasmic 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). | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.645 |
| lolA | pal | STM0961 | STM0749 | Periplasmic 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). | Tol protein required for outer membrane integrity; 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. | 0.782 |
| lolA | ycfU | STM0961 | STM1217 | Periplasmic 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). | Integral membrane protein ABC transporter; Similar to E. coli orf, hypothetical protein (AAC74200.1); Blastp hit to AAC74200.1 (399 aa), 93% identity in aa 1 - 399. | 0.908 |
| lpp | lolA | STM1377 | STM0961 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Periplasmic 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). | 0.773 |
| lpp | lppB | STM1377 | STM1376 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | 0.725 |
| lpp | msbB | STM1377 | STM1889 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | 0.453 |
| lpp | ompA | STM1377 | STM1070 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.946 |
| lpp | pal | STM1377 | STM0749 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Tol protein required for outer membrane integrity; 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. | 0.921 |
| lpp | tonB | STM1377 | STM1737 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...] | 0.579 |
| lpp | ycfU | STM1377 | STM1217 | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Integral membrane protein ABC transporter; Similar to E. coli orf, hypothetical protein (AAC74200.1); Blastp hit to AAC74200.1 (399 aa), 93% identity in aa 1 - 399. | 0.508 |
| lppB | STM1254 | STM1376 | STM1254 | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Putative outer membrane lipoprotein. | 0.511 |
| lppB | STM3216 | STM1376 | STM3216 | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Similar to E. coli methyl-accepting chemotaxis protein I, serine sensor receptor (AAC77311.1); Blastp hit to AAC77311.1 (551 aa), 36% identity in aa 2 - 523. | 0.699 |
| lppB | lolA | STM1376 | STM0961 | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Periplasmic 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). | 0.603 |
| lppB | lpp | STM1376 | STM1377 | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Murein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | 0.725 |
| lppB | msbB | STM1376 | STM1889 | Putative methyl-accepting chemotaxis protein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | 0.455 |