| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dhbB | dhbF | BSU31970 | BSU31960 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | 0.999 |
| dhbB | ppsB | BSU31970 | BSU18330 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.803 |
| dhbB | srfAA | BSU31970 | BSU03480 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.925 |
| dhbB | srfAB | BSU31970 | BSU03490 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.946 |
| dhbB | srfAC | BSU31970 | BSU03510 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Surfactin synthetase; Probably activates a leucine. | 0.965 |
| dhbB | yeeG | BSU31970 | BSU06820 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Putative phage receptor protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.791 |
| dhbF | dhbB | BSU31960 | BSU31970 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.999 |
| dhbF | ppsB | BSU31960 | BSU18330 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.861 |
| dhbF | srfAA | BSU31960 | BSU03480 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.917 |
| dhbF | srfAB | BSU31960 | BSU03490 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.915 |
| dhbF | srfAC | BSU31960 | BSU03510 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Surfactin synthetase; Probably activates a leucine. | 0.825 |
| dhbF | yeeG | BSU31960 | BSU06820 | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | Putative phage receptor protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.449 |
| phrH | rapH | BSU06839 | BSU06830 | Hexapeptide inhibitor of regulatory cascade; Inhibitor of the activity of phosphatase RapH. May inhibit the rapH promoter after import into the cytoplasm. | Response regulator aspartate phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the RAP family. | 0.998 |
| phrH | yeeG | BSU06839 | BSU06820 | Hexapeptide inhibitor of regulatory cascade; Inhibitor of the activity of phosphatase RapH. May inhibit the rapH promoter after import into the cytoplasm. | Putative phage receptor protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.467 |
| ppsB | dhbB | BSU18330 | BSU31970 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.803 |
| ppsB | dhbF | BSU18330 | BSU31960 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin synthetase; Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains. | 0.861 |
| ppsB | srfAA | BSU18330 | BSU03480 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.928 |
| ppsB | srfAB | BSU18330 | BSU03490 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Surfactin synthetase; This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. | 0.959 |
| ppsB | srfAC | BSU18330 | BSU03510 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Surfactin synthetase; Probably activates a leucine. | 0.870 |
| ppsB | yeeG | BSU18330 | BSU06820 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Putative phage receptor protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.525 |