node1 | node2 | node1 annotation | node2 annotation | score |
PSM36_1054 | PSM36_1055 | Ferredoxin-type protein NapF; High confidence in function and specificity. | Hypothetical protein; High confidence in function and specificity. | 0.915 |
PSM36_1054 | PSM36_1056 | Ferredoxin-type protein NapF; High confidence in function and specificity. | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | 0.589 |
PSM36_1054 | PSM36_1057 | Ferredoxin-type protein NapF; High confidence in function and specificity. | Phosphoribosyl transferase domain; High confidence in function and specificity. | 0.463 |
PSM36_1054 | PSM36_1058 | Ferredoxin-type protein NapF; High confidence in function and specificity. | Hypothetical protein; High confidence in function and specificity. | 0.442 |
PSM36_1055 | PSM36_1054 | Hypothetical protein; High confidence in function and specificity. | Ferredoxin-type protein NapF; High confidence in function and specificity. | 0.915 |
PSM36_1055 | PSM36_1056 | Hypothetical protein; High confidence in function and specificity. | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | 0.474 |
PSM36_1055 | PSM36_1057 | Hypothetical protein; High confidence in function and specificity. | Phosphoribosyl transferase domain; High confidence in function and specificity. | 0.436 |
PSM36_1055 | PSM36_1058 | Hypothetical protein; High confidence in function and specificity. | Hypothetical protein; High confidence in function and specificity. | 0.459 |
PSM36_1056 | PSM36_1054 | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | Ferredoxin-type protein NapF; High confidence in function and specificity. | 0.589 |
PSM36_1056 | PSM36_1055 | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | Hypothetical protein; High confidence in function and specificity. | 0.474 |
PSM36_1056 | PSM36_1057 | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | Phosphoribosyl transferase domain; High confidence in function and specificity. | 0.571 |
PSM36_1056 | PSM36_1058 | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | Hypothetical protein; High confidence in function and specificity. | 0.614 |
PSM36_1057 | PSM36_1054 | Phosphoribosyl transferase domain; High confidence in function and specificity. | Ferredoxin-type protein NapF; High confidence in function and specificity. | 0.463 |
PSM36_1057 | PSM36_1055 | Phosphoribosyl transferase domain; High confidence in function and specificity. | Hypothetical protein; High confidence in function and specificity. | 0.436 |
PSM36_1057 | PSM36_1056 | Phosphoribosyl transferase domain; High confidence in function and specificity. | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | 0.571 |
PSM36_1057 | PSM36_1058 | Phosphoribosyl transferase domain; High confidence in function and specificity. | Hypothetical protein; High confidence in function and specificity. | 0.797 |
PSM36_1057 | PSM36_1059 | Phosphoribosyl transferase domain; High confidence in function and specificity. | Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include mem [...] | 0.412 |
PSM36_1058 | PSM36_1054 | Hypothetical protein; High confidence in function and specificity. | Ferredoxin-type protein NapF; High confidence in function and specificity. | 0.442 |
PSM36_1058 | PSM36_1055 | Hypothetical protein; High confidence in function and specificity. | Hypothetical protein; High confidence in function and specificity. | 0.459 |
PSM36_1058 | PSM36_1056 | Hypothetical protein; High confidence in function and specificity. | TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors; High confidence in fun [...] | 0.614 |