node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
bamA | btuB | b0177 | b3966 | 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 Ba [...] | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | 0.687 |
bamA | lamB | b0177 | b4036 | 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 Ba [...] | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | 0.813 |
bamA | ompA | b0177 | b0957 | 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 Ba [...] | Outer membrane protein A (3a;II*;G;d); 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, whic [...] | 0.985 |
bamA | ompC | b0177 | b2215 | 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 Ba [...] | 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; Belongs to the Gram-negative porin family. | 0.970 |
bamA | ompX | b0177 | b0814 | 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 Ba [...] | Outer membrane protein X; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpX family. | 0.699 |
bamA | pldA | b0177 | b3821 | 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 Ba [...] | Outer membrane phospholipase A; Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins. | 0.961 |
bamA | tsx | b0177 | b0411 | 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 Ba [...] | Nucleoside channel, receptor of phage T6 and colicin K; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases. In addition, constitutes the receptor for colicin K and phage T6. Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. | 0.743 |
btuB | bamA | b3966 | b0177 | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | 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 Ba [...] | 0.687 |
btuB | lamB | b3966 | b4036 | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | 0.868 |
btuB | ompA | b3966 | b0957 | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | Outer membrane protein A (3a;II*;G;d); 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, whic [...] | 0.883 |
btuB | ompC | b3966 | b2215 | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | 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; Belongs to the Gram-negative porin family. | 0.870 |
btuB | ompX | b3966 | b0814 | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | Outer membrane protein X; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpX family. | 0.508 |
btuB | tsx | b3966 | b0411 | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | Nucleoside channel, receptor of phage T6 and colicin K; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases. In addition, constitutes the receptor for colicin K and phage T6. Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. | 0.913 |
lamB | bamA | b4036 | b0177 | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | 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 Ba [...] | 0.813 |
lamB | btuB | b4036 | b3966 | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. | 0.868 |
lamB | ompA | b4036 | b0957 | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | Outer membrane protein A (3a;II*;G;d); 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, whic [...] | 0.952 |
lamB | ompC | b4036 | b2215 | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | 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; Belongs to the Gram-negative porin family. | 0.993 |
lamB | ompX | b4036 | b0814 | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | Outer membrane protein X; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpX family. | 0.806 |
lamB | tsx | b4036 | b0411 | Maltose outer membrane porin (maltoporin); Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | Nucleoside channel, receptor of phage T6 and colicin K; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases. In addition, constitutes the receptor for colicin K and phage T6. Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. | 0.974 |
mipA | tsx | b1782 | b0411 | Scaffolding protein for murein synthesizing machinery; May serve as a scaffold protein required for the formation of a complex with MrcB/PonB and MltA, this complex could play a role in enlargement and septation of the murein sacculus. | Nucleoside channel, receptor of phage T6 and colicin K; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases. In addition, constitutes the receptor for colicin K and phage T6. Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. | 0.496 |