node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Sbal_1642 | mltF | Sbal_1642 | Sbal_2981 | PFAM: MotA/TolQ/ExbB proton channel; KEGG: she:Shewmr4_2462 MotA/TolQ/ExbB proton channel. | 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. | 0.409 |
Sbal_1995 | Sbal_2273 | Sbal_1995 | Sbal_2273 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: shn:Shewana3_2370 MLTD_N domain protein. | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | 0.566 |
Sbal_1995 | mltF | Sbal_1995 | Sbal_2981 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: shn:Shewana3_2370 MLTD_N domain 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. | 0.487 |
Sbal_2273 | Sbal_1995 | Sbal_2273 | Sbal_1995 | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: shn:Shewana3_2370 MLTD_N domain protein. | 0.566 |
Sbal_2273 | Sbal_3737 | Sbal_2273 | Sbal_3737 | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO4017 transglycosylase, Slt family. | 0.414 |
Sbal_2273 | mltF | Sbal_2273 | Sbal_2981 | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | 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. | 0.438 |
Sbal_2803 | mltF | Sbal_2803 | Sbal_2981 | KEGG: shn:Shewana3_1417 conserved 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. | 0.843 |
Sbal_3737 | Sbal_2273 | Sbal_3737 | Sbal_2273 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO4017 transglycosylase, Slt family. | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | 0.414 |
Sbal_3737 | mltF | Sbal_3737 | Sbal_2981 | 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. | 0.619 |
Sbal_3737 | rlpA-2 | Sbal_3737 | Sbal_3278 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase, catalytic; MLTD_N domain protein; KEGG: son:SO4017 transglycosylase, Slt family. | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.406 |
mltF | Sbal_1642 | Sbal_2981 | Sbal_1642 | 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: she:Shewmr4_2462 MotA/TolQ/ExbB proton channel. | 0.409 |
mltF | Sbal_1995 | Sbal_2981 | Sbal_1995 | 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: shn:Shewana3_2370 MLTD_N domain protein. | 0.487 |
mltF | Sbal_2273 | Sbal_2981 | Sbal_2273 | 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: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | 0.438 |
mltF | Sbal_2803 | Sbal_2981 | Sbal_2803 | 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: shn:Shewana3_1417 conserved hypothetical protein. | 0.843 |
mltF | Sbal_3737 | Sbal_2981 | Sbal_3737 | 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. | 0.619 |
mltF | nudJ | Sbal_2981 | Sbal_2477 | 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: shn:Shewana3_1748 NUDIX hydrolase; Belongs to the Nudix hydrolase family. NudJ subfamily. | 0.426 |
mltF | purL | Sbal_2981 | Sbal_2980 | 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-2 | Sbal_2981 | Sbal_3278 | 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. | 0.441 |
nudJ | mltF | Sbal_2477 | Sbal_2981 | PFAM: NUDIX hydrolase; KEGG: shn:Shewana3_1748 NUDIX hydrolase; 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. | 0.426 |
purL | mltF | Sbal_2980 | Sbal_2981 | 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 |