| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bamA | lnt | b0177 | b0657 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | 0.527 |
| bamA | lolA | b0177 | b0891 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | 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 | 0.969 |
| bamA | lolB | b0177 | b1209 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | 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 | 0.944 |
| bamA | lolC | b0177 | b1116 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Lipoprotein release complex - inner membrane subunit; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA | 0.902 |
| bamA | lolD | b0177 | b1117 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA | 0.736 |
| bamA | lolE | b0177 | b1118 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Lipoprotein release complex - inner membrane subunit; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA | 0.822 |
| bamA | lspA | b0177 | b0027 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Prolipoprotein signal peptidase (signal peptidase ii); This protein specifically catalyzes the removal of signal peptides from prolipoproteins | 0.641 |
| bamA | macB | b0177 | b0879 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | Abc-type tripartite efflux pump atp binding/membrane subunit; 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. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid | 0.453 |
| bamA | pal | b0177 | b0741 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | 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 | 0.900 |
| lnt | bamA | b0657 | b0177 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | 0.527 |
| lnt | lolA | b0657 | b0891 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | 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 | 0.941 |
| lnt | lolB | b0657 | b1209 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | 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 | 0.919 |
| lnt | lolC | b0657 | b1116 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | Lipoprotein release complex - inner membrane subunit; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA | 0.882 |
| lnt | lolD | b0657 | b1117 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA | 0.500 |
| lnt | lolE | b0657 | b1118 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | Lipoprotein release complex - inner membrane subunit; Part of an ATP-dependent transport system LolCDE responsible for the release of lipoproteins targeted to the outer membrane from the inner membrane. Such a release is dependent of the sorting-signal (absence of an Asp at position 2 of the mature lipoprotein) and of LolA | 0.822 |
| lnt | lspA | b0657 | b0027 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | Prolipoprotein signal peptidase (signal peptidase ii); This protein specifically catalyzes the removal of signal peptides from prolipoproteins | 0.963 |
| lnt | macB | b0657 | b0879 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | Abc-type tripartite efflux pump atp binding/membrane subunit; 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. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, the system could also transport R-LPS or a similar glycolipid | 0.512 |
| lnt | pal | b0657 | b0741 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | 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 | 0.613 |
| lolA | bamA | b0891 | b0177 | 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 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam [...] | 0.969 |
| lolA | lnt | b0891 | b0657 | 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 | Apolipoprotein n-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation Utilizes a two-step reaction via a ping-pong mechanism . Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein . In vitro, can utilize the phospholipids phosphatidylethanolam [...] | 0.941 |
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