| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | yweA | BSU31970 | BSU37800 | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Member of the processed secretome; Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity. | 0.814 |
| gmuD | yweA | BSU05840 | BSU37800 | Mannoside-phospho-beta-d-glucosidase; Phospho-beta-D-glucosidase that seems to be involved in the degradation of glucomannan. Is also capable of hydrolyzing aryl- phospho-beta-D-glucosides, although very weakly, and plays only a minor role, if any, in the degradation of these substrates in vivo. Belongs to the glycosyl hydrolase 1 family. | Member of the processed secretome; Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity. | 0.519 |
| nucB | ylqB | BSU25750 | BSU15960 | Nuclease; Degrades both double-stranded linear and covalently closed circular DNA. Likely to play a scavenging role in order to supply nutrients under starvation conditions; To B.subtilis NucA/ComI. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15033535. | 0.747 |
| nucB | yweA | BSU25750 | BSU37800 | Nuclease; Degrades both double-stranded linear and covalently closed circular DNA. Likely to play a scavenging role in order to supply nutrients under starvation conditions; To B.subtilis NucA/ComI. | Member of the processed secretome; Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity. | 0.519 |
| 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 | 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 | yweA | BSU18330 | BSU37800 | 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. | Member of the processed secretome; Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity. | 0.604 |
| rocG | yweA | BSU37790 | BSU37800 | Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...] | Member of the processed secretome; Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity. | 0.715 |
| srfAA | dhbB | BSU03480 | BSU31970 | 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. | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.925 |
| srfAA | ppsB | BSU03480 | BSU18330 | 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. | 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. | 0.928 |
| srfAA | srfAB | BSU03480 | BSU03490 | 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. | 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. | 0.999 |
| srfAA | srfAC | BSU03480 | BSU03510 | 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. | Surfactin synthetase; Probably activates a leucine. | 0.999 |
| srfAA | yweA | BSU03480 | BSU37800 | 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. | Member of the processed secretome; Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity. | 0.634 |
| srfAB | dhbB | BSU03490 | BSU31970 | 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. | Isochorismatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.946 |
