| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMF97216.1 | AMF98409.1 | AL538_05365 | AL538_12105 | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.458 |
| AMF98409.1 | AMF97216.1 | AL538_12105 | AL538_05365 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Lytic transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.458 |
| AMF98409.1 | AMF98412.1 | AL538_12105 | AL538_12120 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.652 |
| AMF98409.1 | AMF98413.1 | AL538_12105 | AL538_12125 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.446 |
| AMF98409.1 | AMF99635.1 | AL538_12105 | AL538_18075 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.400 |
| AMF98409.1 | AMG00399.1 | AL538_12105 | AL538_22185 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Transglycosylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.485 |
| AMF98409.1 | AMG00942.1 | AL538_12105 | AL538_25100 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Permease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.414 |
| AMF98409.1 | bamD | AL538_12105 | AL538_12110 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Hypothetical protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.729 |
| AMF98409.1 | purL | AL538_12105 | AL538_12780 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.404 |
| AMF98409.1 | raiA | AL538_12105 | AL538_12100 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | Cold-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.509 |
| AMF98409.1 | rluD | AL538_12105 | AL538_12115 | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 23S rRNA pseudouridylate synthase; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.652 |
| AMF98412.1 | AMF98409.1 | AL538_12120 | AL538_12105 | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.652 |
| AMF98412.1 | AMF98413.1 | AL538_12120 | AL538_12125 | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.715 |
| AMF98412.1 | bamD | AL538_12120 | AL538_12110 | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.744 |
| AMF98412.1 | raiA | AL538_12120 | AL538_12100 | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cold-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.578 |
| AMF98412.1 | rluD | AL538_12120 | AL538_12115 | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 23S rRNA pseudouridylate synthase; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.893 |
| AMF98413.1 | AMF98409.1 | AL538_12125 | AL538_12105 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Amino acid ABC transporter substrate-binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. | 0.446 |
| AMF98413.1 | AMF98412.1 | AL538_12125 | AL538_12120 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Polyphenol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.715 |
| AMF98413.1 | bamD | AL538_12125 | AL538_12110 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Hypothetical protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.644 |
| AMF98413.1 | raiA | AL538_12125 | AL538_12100 | ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Cold-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.408 |
