| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EGJ26388.1 | dltA | STRPO_0108 | STRPO_0109 | Hypothetical protein. | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | 0.770 |
| EGJ26388.1 | dltB | STRPO_0108 | STRPO_0110 | Hypothetical protein. | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | 0.763 |
| EGJ26388.1 | dltC | STRPO_0108 | STRPO_0111 | Hypothetical protein. | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | 0.736 |
| EGJ26388.1 | dltD | STRPO_0108 | STRPO_0112 | Hypothetical protein. | DltD C-terminal domain protein; Identified by match to protein family HMM PF04914; match to protein family HMM PF04915; match to protein family HMM PF04918. | 0.736 |
| EGJ26388.1 | uvrB | STRPO_0108 | STRPO_0107 | Hypothetical protein. | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.464 |
| dltA | EGJ26388.1 | STRPO_0109 | STRPO_0108 | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | Hypothetical protein. | 0.770 |
| dltA | dltB | STRPO_0109 | STRPO_0110 | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | 0.997 |
| dltA | dltC | STRPO_0109 | STRPO_0111 | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | 0.999 |
| dltA | dltD | STRPO_0109 | STRPO_0112 | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | DltD C-terminal domain protein; Identified by match to protein family HMM PF04914; match to protein family HMM PF04915; match to protein family HMM PF04918. | 0.996 |
| dltA | uvrB | STRPO_0109 | STRPO_0107 | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.440 |
| dltB | EGJ26388.1 | STRPO_0110 | STRPO_0108 | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | Hypothetical protein. | 0.763 |
| dltB | dltA | STRPO_0110 | STRPO_0109 | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | 0.997 |
| dltB | dltC | STRPO_0110 | STRPO_0111 | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | 0.999 |
| dltB | dltD | STRPO_0110 | STRPO_0112 | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | DltD C-terminal domain protein; Identified by match to protein family HMM PF04914; match to protein family HMM PF04915; match to protein family HMM PF04918. | 0.998 |
| dltB | uvrB | STRPO_0110 | STRPO_0107 | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.441 |
| dltC | EGJ26388.1 | STRPO_0111 | STRPO_0108 | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | Hypothetical protein. | 0.736 |
| dltC | dltA | STRPO_0111 | STRPO_0109 | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | D-alanine--poly(phosphoribitol) ligase, subunit 1; 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 [...] | 0.999 |
| dltC | dltB | STRPO_0111 | STRPO_0110 | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | Protein DltB; Could be involved in the transport of activated D-alanine through the membrane. | 0.999 |
| dltC | dltD | STRPO_0111 | STRPO_0112 | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | DltD C-terminal domain protein; Identified by match to protein family HMM PF04914; match to protein family HMM PF04915; match to protein family HMM PF04918. | 0.997 |
| dltC | uvrB | STRPO_0111 | STRPO_0107 | D-alanine--poly(phosphoribitol) ligase, subunit 2; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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. | Excinuclease ABC, B subunit; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] | 0.418 |