node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACA73953.1 | ACA74205.1 | PputW619_3470 | PputW619_3723 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: pen:PSEEN3562 membrane-bound lytic murein transglycosylase D MltD. | KEGG: pen:PSEEN3833 peptidoglycan hydrolase FlgJ; TIGRFAM: flagellar rod assembly protein/muramidase FlgJ; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase; SMART: Lysozyme subfamily 2. | 0.490 |
ACA73953.1 | mltF | PputW619_3470 | PputW619_4190 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: pen:PSEEN3562 membrane-bound lytic murein transglycosylase D MltD. | 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. | 0.494 |
ACA73953.1 | rlpA | PputW619_3470 | PputW619_0617 | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: pen:PSEEN3562 membrane-bound lytic murein transglycosylase D MltD. | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.627 |
ACA74205.1 | ACA73953.1 | PputW619_3723 | PputW619_3470 | KEGG: pen:PSEEN3833 peptidoglycan hydrolase FlgJ; TIGRFAM: flagellar rod assembly protein/muramidase FlgJ; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase; SMART: Lysozyme subfamily 2. | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: pen:PSEEN3562 membrane-bound lytic murein transglycosylase D MltD. | 0.490 |
ACA74205.1 | mltF | PputW619_3723 | PputW619_4190 | KEGG: pen:PSEEN3833 peptidoglycan hydrolase FlgJ; TIGRFAM: flagellar rod assembly protein/muramidase FlgJ; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase; SMART: Lysozyme subfamily 2. | 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. | 0.400 |
ACA74668.1 | mltF | PputW619_4188 | PputW619_4190 | KEGG: pen:PSEEN4385 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. | 0.556 |
ACA74668.1 | purL | PputW619_4188 | PputW619_4189 | KEGG: pen:PSEEN4385 hypothetical protein. | 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. | 0.827 |
ACA75397.1 | mltF | PputW619_4921 | PputW619_4190 | PFAM: AsmA family protein; KEGG: pen:PSEEN5198 AsmA 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. | 0.434 |
mltF | ACA73953.1 | PputW619_4190 | PputW619_3470 | 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: pen:PSEEN3562 membrane-bound lytic murein transglycosylase D MltD. | 0.494 |
mltF | ACA74205.1 | PputW619_4190 | PputW619_3723 | 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: pen:PSEEN3833 peptidoglycan hydrolase FlgJ; TIGRFAM: flagellar rod assembly protein/muramidase FlgJ; PFAM: Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase; SMART: Lysozyme subfamily 2. | 0.400 |
mltF | ACA74668.1 | PputW619_4190 | PputW619_4188 | 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: pen:PSEEN4385 hypothetical protein. | 0.556 |
mltF | ACA75397.1 | PputW619_4190 | PputW619_4921 | 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: AsmA family protein; KEGG: pen:PSEEN5198 AsmA protein. | 0.434 |
mltF | purL | PputW619_4190 | PputW619_4189 | 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. | 0.793 |
mltF | rlpA | PputW619_4190 | PputW619_0617 | 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. | 0.443 |
purL | ACA74668.1 | PputW619_4189 | PputW619_4188 | 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. | KEGG: pen:PSEEN4385 hypothetical protein. | 0.827 |
purL | mltF | PputW619_4189 | PputW619_4190 | 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. | 0.793 |
rlpA | ACA73953.1 | PputW619_0617 | PputW619_3470 | Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | MLTD_N domain protein; PFAM: Peptidoglycan-binding LysM; Lytic transglycosylase catalytic; MLTD_N domain protein; KEGG: pen:PSEEN3562 membrane-bound lytic murein transglycosylase D MltD. | 0.627 |
rlpA | mltF | PputW619_0617 | PputW619_4190 | 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. | 0.443 |