node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
lolA | lolB | b0891 | b1209 | 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); the inner membrane retention signal functions at the release step | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | 0.999 |
lolA | lpp | b0891 | b1677 | 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); the inner membrane retention signal functions at the release step | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | 0.885 |
lolA | lspA | b0891 | b0027 | 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); the inner membrane retention signal functions at the release step | Prolipoprotein signal peptidase (signal peptidase ii); This protein specifically catalyzes the removal of signal peptides from prolipoproteins | 0.901 |
lolA | ompA | b0891 | b0957 | 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); the inner membrane retention signal functions at the release step | With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape . Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes . A very abundant protein, there can be up to 210,000 OmpA molecules per cell . Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at [...] | 0.670 |
lolA | ompC | b0891 | b2215 | 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); the inner membrane retention signal functions at the release step | Outer membrane porin protein c; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity | 0.572 |
lolA | ompF | b0891 | b0929 | 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); the inner membrane retention signal functions at the release step | Outer membrane porin 1a (ia;b;f); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity | 0.526 |
lolA | pal | b0891 | b0741 | 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); the inner membrane retention signal functions at the release step | Peptidoglycan-associated outer membrane lipoprotein pal; 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 The Tol-Pal system is also required for polar localization of chemoreceptors clusters | 0.939 |
lolA | tolB | b0891 | b0740 | 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); the inner membrane retention signal functions at the release step | Tol-pal system periplasmic protein tolb; 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 . TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane . Is also involved in the uptake of some colicins A The Tol-Pal system is also required for polar localization of chemoreceptors clusters | 0.851 |
lolB | lolA | b1209 | b0891 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | 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); the inner membrane retention signal functions at the release step | 0.999 |
lolB | lpp | b1209 | b1677 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | 0.837 |
lolB | lspA | b1209 | b0027 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | Prolipoprotein signal peptidase (signal peptidase ii); This protein specifically catalyzes the removal of signal peptides from prolipoproteins | 0.892 |
lolB | pal | b1209 | b0741 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | Peptidoglycan-associated outer membrane lipoprotein pal; 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 The Tol-Pal system is also required for polar localization of chemoreceptors clusters | 0.884 |
lolB | rcsF | b1209 | b0196 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | Outer membrane lipoprotein rcsf; Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division | 0.758 |
lolB | tolB | b1209 | b0740 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | Tol-pal system periplasmic protein tolb; 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 . TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane . Is also involved in the uptake of some colicins A The Tol-Pal system is also required for polar localization of chemoreceptors clusters | 0.632 |
lolB | tonB | b1209 | b1252 | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | Membrane spanning protein in tonb-exbb-exbd transport complex; 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 tran [...] | 0.510 |
lpp | lolA | b1677 | b0891 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | 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); the inner membrane retention signal functions at the release step | 0.885 |
lpp | lolB | b1677 | b1209 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability | 0.837 |
lpp | lspA | b1677 | b0027 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | Prolipoprotein signal peptidase (signal peptidase ii); This protein specifically catalyzes the removal of signal peptides from prolipoproteins | 0.851 |
lpp | ompA | b1677 | b0957 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape . Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes . A very abundant protein, there can be up to 210,000 OmpA molecules per cell . Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at [...] | 0.989 |
lpp | ompC | b1677 | b2215 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . 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 the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...] | Outer membrane porin protein c; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity | 0.773 |