node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABK47651.1 | mltF | Shewana3_1417 | Shewana3_1239 | KEGG: son:SO3132 hypothetical protein. | Lytic transglycosylase, catalytic; 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. | 0.673 |
ABK48599.1 | mltF | Shewana3_2370 | Shewana3_1239 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO2564 transglycosylase, Slt family. | Lytic transglycosylase, catalytic; 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. | 0.524 |
ABK48851.1 | mltF | Shewana3_2624 | Shewana3_1239 | PFAM: MotA/TolQ/ExbB proton channel; KEGG: son:SO1826 TonB system transport protein ExbB2. | Lytic transglycosylase, catalytic; 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. | 0.424 |
ABK49806.1 | mltF | Shewana3_3584 | Shewana3_1239 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO4017 transglycosylase, Slt family. | Lytic transglycosylase, catalytic; 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. | 0.644 |
mltF | ABK47651.1 | Shewana3_1239 | Shewana3_1417 | Lytic transglycosylase, catalytic; 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. | KEGG: son:SO3132 hypothetical protein. | 0.673 |
mltF | ABK48599.1 | Shewana3_1239 | Shewana3_2370 | Lytic transglycosylase, catalytic; 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. | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO2564 transglycosylase, Slt family. | 0.524 |
mltF | ABK48851.1 | Shewana3_1239 | Shewana3_2624 | Lytic transglycosylase, catalytic; 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. | PFAM: MotA/TolQ/ExbB proton channel; KEGG: son:SO1826 TonB system transport protein ExbB2. | 0.424 |
mltF | ABK49806.1 | Shewana3_1239 | Shewana3_3584 | Lytic transglycosylase, catalytic; 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. | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO4017 transglycosylase, Slt family. | 0.644 |
mltF | nudJ | Shewana3_1239 | Shewana3_1748 | Lytic transglycosylase, catalytic; 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. | PFAM: NUDIX hydrolase; KEGG: son:SO2631 MutT/nudix family protein; Belongs to the Nudix hydrolase family. NudJ subfamily. | 0.427 |
mltF | purL | Shewana3_1239 | Shewana3_1240 | Lytic transglycosylase, catalytic; 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. | 0.747 |
mltF | rlpA | Shewana3_1239 | Shewana3_0992 | Lytic transglycosylase, catalytic; 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. | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.413 |
nudJ | mltF | Shewana3_1748 | Shewana3_1239 | PFAM: NUDIX hydrolase; KEGG: son:SO2631 MutT/nudix family protein; Belongs to the Nudix hydrolase family. NudJ subfamily. | Lytic transglycosylase, catalytic; 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. | 0.427 |
purL | mltF | Shewana3_1240 | Shewana3_1239 | 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. | Lytic transglycosylase, catalytic; 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. | 0.747 |
rlpA | mltF | Shewana3_0992 | Shewana3_1239 | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | Lytic transglycosylase, catalytic; 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. | 0.413 |