| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dltA | mprF | SAOUHSC_00869 | SAOUHSC_01359 | D-alanine-activating enzyme; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP-dependent AMP [...] | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | 0.799 |
| dltA | oatA | SAOUHSC_00869 | SAOUHSC_02885 | D-alanine-activating enzyme; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP-dependent AMP [...] | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | 0.500 |
| mprF | dltA | SAOUHSC_01359 | SAOUHSC_00869 | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | D-alanine-activating enzyme; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP-dependent AMP [...] | 0.799 |
| mprF | oatA | SAOUHSC_01359 | SAOUHSC_02885 | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | 0.601 |
| mprF | sceD | SAOUHSC_01359 | SAOUHSC_02333 | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | sceD protein, putative; Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. Is required for normal growth under stressful conditions. Is essential for nasal colonization. Belongs to the transglycosylase family. SceD subfamily. | 0.403 |
| mprF | srtA | SAOUHSC_01359 | SAOUHSC_02834 | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | Sortase, putative; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the disp [...] | 0.638 |
| mprF | ssaA | SAOUHSC_01359 | SAOUHSC_02883 | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | LysM domain protein; Not known; immunogenic protein. | 0.415 |
| oatA | dltA | SAOUHSC_02885 | SAOUHSC_00869 | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | D-alanine-activating enzyme; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP-dependent AMP [...] | 0.500 |
| oatA | mprF | SAOUHSC_02885 | SAOUHSC_01359 | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | 0.601 |
| oatA | sceD | SAOUHSC_02885 | SAOUHSC_02333 | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | sceD protein, putative; Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. Is required for normal growth under stressful conditions. Is essential for nasal colonization. Belongs to the transglycosylase family. SceD subfamily. | 0.400 |
| oatA | srtA | SAOUHSC_02885 | SAOUHSC_02834 | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | Sortase, putative; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the disp [...] | 0.471 |
| oatA | ssaA | SAOUHSC_02885 | SAOUHSC_02883 | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | LysM domain protein; Not known; immunogenic protein. | 0.465 |
| sceD | mprF | SAOUHSC_02333 | SAOUHSC_01359 | sceD protein, putative; Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. Is required for normal growth under stressful conditions. Is essential for nasal colonization. Belongs to the transglycosylase family. SceD subfamily. | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | 0.403 |
| sceD | oatA | SAOUHSC_02333 | SAOUHSC_02885 | sceD protein, putative; Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. Is required for normal growth under stressful conditions. Is essential for nasal colonization. Belongs to the transglycosylase family. SceD subfamily. | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | 0.400 |
| sceD | ssaA | SAOUHSC_02333 | SAOUHSC_02883 | sceD protein, putative; Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. Is required for normal growth under stressful conditions. Is essential for nasal colonization. Belongs to the transglycosylase family. SceD subfamily. | LysM domain protein; Not known; immunogenic protein. | 0.558 |
| srtA | mprF | SAOUHSC_02834 | SAOUHSC_01359 | Sortase, putative; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the disp [...] | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | 0.638 |
| srtA | oatA | SAOUHSC_02834 | SAOUHSC_02885 | Sortase, putative; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the disp [...] | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | 0.471 |
| ssaA | mprF | SAOUHSC_02883 | SAOUHSC_01359 | LysM domain protein; Not known; immunogenic protein. | Conserved hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively [...] | 0.415 |
| ssaA | oatA | SAOUHSC_02883 | SAOUHSC_02885 | LysM domain protein; Not known; immunogenic protein. | Conserved hypothetical protein; Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. Belongs to the acyltransferase 3 family. | 0.465 |
| ssaA | sceD | SAOUHSC_02883 | SAOUHSC_02333 | LysM domain protein; Not known; immunogenic protein. | sceD protein, putative; Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. Is required for normal growth under stressful conditions. Is essential for nasal colonization. Belongs to the transglycosylase family. SceD subfamily. | 0.558 |
