| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cwlC | pbpA | BSU17410 | BSU25000 | N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | Transpeptidase (penicillin-binding protein 2A); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.489 |
| cwlC | pbpB | BSU17410 | BSU15160 | N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | Penicillin-binding protein 2B; Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis; Belongs to the transpeptidase family. | 0.562 |
| cwlC | pbpF | BSU17410 | BSU10110 | N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | Penicillin-binding protein 2C required for spore germination; Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall; In the N-terminal section; belongs to the glycosyltransferase 51 family. | 0.778 |
| cwlC | ponA | BSU17410 | BSU22320 | N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | Peptidoglycan glycosyltransferase (penicillin-binding proteins 1A and 1B); Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.807 |
| cwlC | rodA | BSU17410 | BSU38120 | N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | Factor involved in extension of the lateral walls of the cell; Peptidoglycan polymerase that is essential for cell wall elongation. Also required for the maintenance of the rod cell shape. Belongs to the SEDS family. MrdB/RodA subfamily. | 0.551 |
| cwlC | spoVD | BSU17410 | BSU15170 | N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. | Penicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. | 0.597 |
| dacA | dacB | BSU00100 | BSU23190 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). | 0.949 |
| dacA | dacF | BSU00100 | BSU23480 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | D-alanyl-D-alanine carboxypeptidase (penicilin binding protein); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | 0.925 |
| dacA | pbpA | BSU00100 | BSU25000 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | Transpeptidase (penicillin-binding protein 2A); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. | 0.662 |
| dacA | pbpB | BSU00100 | BSU15160 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | Penicillin-binding protein 2B; Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis; Belongs to the transpeptidase family. | 0.785 |
| dacA | pbpF | BSU00100 | BSU10110 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | Penicillin-binding protein 2C required for spore germination; Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall; In the N-terminal section; belongs to the glycosyltransferase 51 family. | 0.932 |
| dacA | ponA | BSU00100 | BSU22320 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | Peptidoglycan glycosyltransferase (penicillin-binding proteins 1A and 1B); Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.987 |
| dacA | rodA | BSU00100 | BSU38120 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | Factor involved in extension of the lateral walls of the cell; Peptidoglycan polymerase that is essential for cell wall elongation. Also required for the maintenance of the rod cell shape. Belongs to the SEDS family. MrdB/RodA subfamily. | 0.804 |
| dacA | spoVD | BSU00100 | BSU15170 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | Penicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. | 0.585 |
| dacA | yodJ | BSU00100 | BSU19620 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | D-alanyl-D-alanine carboxypeptidase lipoprotein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.914 |
| dacB | dacA | BSU23190 | BSU00100 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. | 0.949 |
| dacB | dacF | BSU23190 | BSU23480 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). | D-alanyl-D-alanine carboxypeptidase (penicilin binding protein); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | 0.926 |
| dacB | pbpF | BSU23190 | BSU10110 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). | Penicillin-binding protein 2C required for spore germination; Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall; In the N-terminal section; belongs to the glycosyltransferase 51 family. | 0.906 |
| dacB | ponA | BSU23190 | BSU22320 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). | Peptidoglycan glycosyltransferase (penicillin-binding proteins 1A and 1B); Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.906 |
| dacB | spoVD | BSU23190 | BSU15170 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex). | Penicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell. | 0.899 |