| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dacC | hxlR | BSU18350 | BSU03470 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Positive regulator of hxlAB expression; Positive regulator of hxlAB expression. | 0.537 |
| dacC | ppsA | BSU18350 | BSU18340 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.506 |
| dacC | ppsD | BSU18350 | BSU18310 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.428 |
| dacC | ppsE | BSU18350 | BSU18300 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.669 |
| dacC | xynD | BSU18350 | BSU18160 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Arabinoxylan arabinofuranohydrolase; Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation. Is more active on wheat bran AXOS than on wheat water-extractable AX and rye water-extractable AX. Does not display endoxylanase, xylosidase or arabinanase activity. | 0.631 |
| dacC | yngK | BSU18350 | BSU18280 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Putative exported protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.589 |
| dacC | yngL | BSU18350 | BSU18290 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.775 |
| dacC | yxjF | BSU18350 | BSU38970 | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | Putative dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.716 |
| hxlR | dacC | BSU03470 | BSU18350 | Positive regulator of hxlAB expression; Positive regulator of hxlAB expression. | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | 0.537 |
| hxlR | yngL | BSU03470 | BSU18290 | Positive regulator of hxlAB expression; Positive regulator of hxlAB expression. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.602 |
| ppsA | dacC | BSU18340 | BSU18350 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | 0.506 |
| ppsA | ppsD | BSU18340 | BSU18310 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | 0.803 |
| ppsA | ppsE | BSU18340 | BSU18300 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.876 |
| ppsA | yngK | BSU18340 | BSU18280 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | Putative exported protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.421 |
| ppsA | yngL | BSU18340 | BSU18290 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.480 |
| ppsD | dacC | BSU18310 | BSU18350 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | 0.428 |
| ppsD | ppsA | BSU18310 | BSU18340 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.803 |
| ppsD | ppsE | BSU18310 | BSU18300 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | 0.967 |
| ppsD | yngL | BSU18310 | BSU18290 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains. Belongs to the ATP-dependent AMP-binding enzyme family. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.518 |
| ppsE | dacC | BSU18300 | BSU18350 | Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family. | D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions. | 0.669 |
