| node1 | node2 | node1 annotation | node2 annotation | score |
| Deba_2435 | Deba_3108 | Lytic transglycosylase catalytic; InterPro IPR002482:IPR008258:IPR018392; KEGG: sfu:Sfum_0750 peptidoglycan-binding LysM; PFAM: Lytic transglycosylase catalytic; Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding LysM; SPTR: A0LG96 Peptidoglycan-binding LysM; PFAM: Transglycosylase SLT domain; LysM domain. | Extracellular solute-binding protein family 3; 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. | 0.463 |
| Deba_3105 | Deba_3106 | GCN5-related N-acetyltransferase; InterPro IPR016181:IPR000182; KEGG: dal:Dalk_4314 hypothetical protein; PFAM: GCN5-related N-acetyltransferase; SPTR: A3HRP2 Putative uncharacterized protein; PFAM: Acetyltransferase (GNAT) family. | Beta-lactamase domain-containing protein; COGs: COG0491 Zn-dependent hydrolase including glyoxylase; KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein; SPTR: Q1NSR0 Beta-lactamase-like; PFAM: Metallo-beta-lactamase superfamily. | 0.486 |
| Deba_3105 | Deba_3108 | GCN5-related N-acetyltransferase; InterPro IPR016181:IPR000182; KEGG: dal:Dalk_4314 hypothetical protein; PFAM: GCN5-related N-acetyltransferase; SPTR: A3HRP2 Putative uncharacterized protein; PFAM: Acetyltransferase (GNAT) family. | Extracellular solute-binding protein family 3; 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. | 0.423 |
| Deba_3106 | Deba_3105 | Beta-lactamase domain-containing protein; COGs: COG0491 Zn-dependent hydrolase including glyoxylase; KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein; SPTR: Q1NSR0 Beta-lactamase-like; PFAM: Metallo-beta-lactamase superfamily. | GCN5-related N-acetyltransferase; InterPro IPR016181:IPR000182; KEGG: dal:Dalk_4314 hypothetical protein; PFAM: GCN5-related N-acetyltransferase; SPTR: A3HRP2 Putative uncharacterized protein; PFAM: Acetyltransferase (GNAT) family. | 0.486 |
| Deba_3106 | Deba_3107 | Beta-lactamase domain-containing protein; COGs: COG0491 Zn-dependent hydrolase including glyoxylase; KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein; SPTR: Q1NSR0 Beta-lactamase-like; PFAM: Metallo-beta-lactamase superfamily. | Hypothetical protein; InterPro IPR006624; KEGG: scl:sce9098 hypothetical protein; SPTR: A9GA14 Putative uncharacterized protein. | 0.529 |
| Deba_3106 | Deba_3108 | Beta-lactamase domain-containing protein; COGs: COG0491 Zn-dependent hydrolase including glyoxylase; KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein; SPTR: Q1NSR0 Beta-lactamase-like; PFAM: Metallo-beta-lactamase superfamily. | Extracellular solute-binding protein family 3; 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. | 0.525 |
| Deba_3107 | Deba_3106 | Hypothetical protein; InterPro IPR006624; KEGG: scl:sce9098 hypothetical protein; SPTR: A9GA14 Putative uncharacterized protein. | Beta-lactamase domain-containing protein; COGs: COG0491 Zn-dependent hydrolase including glyoxylase; KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein; SPTR: Q1NSR0 Beta-lactamase-like; PFAM: Metallo-beta-lactamase superfamily. | 0.529 |
| Deba_3107 | Deba_3108 | Hypothetical protein; InterPro IPR006624; KEGG: scl:sce9098 hypothetical protein; SPTR: A9GA14 Putative uncharacterized protein. | Extracellular solute-binding protein family 3; 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. | 0.746 |
| Deba_3108 | Deba_2435 | Extracellular solute-binding protein family 3; 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 catalytic; InterPro IPR002482:IPR008258:IPR018392; KEGG: sfu:Sfum_0750 peptidoglycan-binding LysM; PFAM: Lytic transglycosylase catalytic; Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding LysM; SPTR: A0LG96 Peptidoglycan-binding LysM; PFAM: Transglycosylase SLT domain; LysM domain. | 0.463 |
| Deba_3108 | Deba_3105 | Extracellular solute-binding protein family 3; 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. | GCN5-related N-acetyltransferase; InterPro IPR016181:IPR000182; KEGG: dal:Dalk_4314 hypothetical protein; PFAM: GCN5-related N-acetyltransferase; SPTR: A3HRP2 Putative uncharacterized protein; PFAM: Acetyltransferase (GNAT) family. | 0.423 |
| Deba_3108 | Deba_3106 | Extracellular solute-binding protein family 3; 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. | Beta-lactamase domain-containing protein; COGs: COG0491 Zn-dependent hydrolase including glyoxylase; KEGG: sfu:Sfum_1732 beta-lactamase domain-containing protein; SPTR: Q1NSR0 Beta-lactamase-like; PFAM: Metallo-beta-lactamase superfamily. | 0.525 |
| Deba_3108 | Deba_3107 | Extracellular solute-binding protein family 3; 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; InterPro IPR006624; KEGG: scl:sce9098 hypothetical protein; SPTR: A9GA14 Putative uncharacterized protein. | 0.746 |