| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD29888.1 | ABD31731.1 | SAOUHSC_00756 | SAOUHSC_02723 | Conserved hypothetical protein. | Glycerate kinase, putative; Belongs to the glycerate kinase type-1 family. | 0.927 |
| ABD29888.1 | cidB | SAOUHSC_00756 | SAOUHSC_02850 | Conserved hypothetical protein. | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.472 |
| ABD31731.1 | ABD29888.1 | SAOUHSC_02723 | SAOUHSC_00756 | Glycerate kinase, putative; Belongs to the glycerate kinase type-1 family. | Conserved hypothetical protein. | 0.927 |
| ABD31731.1 | cidB | SAOUHSC_02723 | SAOUHSC_02850 | Glycerate kinase, putative; Belongs to the glycerate kinase type-1 family. | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.472 |
| ABD31849.1 | ABD31852.1 | SAOUHSC_02849 | SAOUHSC_02852 | Pyruvate oxidase, putative; Belongs to the TPP enzyme family. | Conserved hypothetical protein; Belongs to the LysR transcriptional regulatory family. | 0.400 |
| ABD31849.1 | cidA | SAOUHSC_02849 | SAOUHSC_02851 | Pyruvate oxidase, putative; Belongs to the TPP enzyme family. | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.756 |
| ABD31849.1 | cidB | SAOUHSC_02849 | SAOUHSC_02850 | Pyruvate oxidase, putative; Belongs to the TPP enzyme family. | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.770 |
| ABD31852.1 | ABD31849.1 | SAOUHSC_02852 | SAOUHSC_02849 | Conserved hypothetical protein; Belongs to the LysR transcriptional regulatory family. | Pyruvate oxidase, putative; Belongs to the TPP enzyme family. | 0.400 |
| ABD31852.1 | cidA | SAOUHSC_02852 | SAOUHSC_02851 | Conserved hypothetical protein; Belongs to the LysR transcriptional regulatory family. | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.704 |
| ABD31852.1 | cidB | SAOUHSC_02852 | SAOUHSC_02850 | Conserved hypothetical protein; Belongs to the LysR transcriptional regulatory family. | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.669 |
| cidA | ABD31849.1 | SAOUHSC_02851 | SAOUHSC_02849 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Pyruvate oxidase, putative; Belongs to the TPP enzyme family. | 0.756 |
| cidA | ABD31852.1 | SAOUHSC_02851 | SAOUHSC_02852 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein; Belongs to the LysR transcriptional regulatory family. | 0.704 |
| cidA | cidB | SAOUHSC_02851 | SAOUHSC_02850 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.985 |
| cidA | lrgA | SAOUHSC_02851 | SAOUHSC_00232 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. Increases tolerance to penicillin possibly by inhibiting the formation of the CidAB holin-like complexes within the membrane, thus reducing penicillin-induced lethality. Possibly plays a role in programmed cell death (PCD), triggering PCD in response to penicillin, and possibly other antibiotics, and environmental stresses. | 0.839 |
| cidB | ABD29888.1 | SAOUHSC_02850 | SAOUHSC_00756 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein. | 0.472 |
| cidB | ABD31731.1 | SAOUHSC_02850 | SAOUHSC_02723 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Glycerate kinase, putative; Belongs to the glycerate kinase type-1 family. | 0.472 |
| cidB | ABD31849.1 | SAOUHSC_02850 | SAOUHSC_02849 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Pyruvate oxidase, putative; Belongs to the TPP enzyme family. | 0.770 |
| cidB | ABD31852.1 | SAOUHSC_02850 | SAOUHSC_02852 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein; Belongs to the LysR transcriptional regulatory family. | 0.669 |
| cidB | cidA | SAOUHSC_02850 | SAOUHSC_02851 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | 0.985 |
| cidB | lrgA | SAOUHSC_02850 | SAOUHSC_00232 | Conserved hypothetical protein; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidAB proteins. When a cell is stressed by the addition of antibiotics or by other factors in the environment, the CidAB proteins possibly oligomerize within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypoth [...] | Conserved hypothetical protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. Increases tolerance to penicillin possibly by inhibiting the formation of the CidAB holin-like complexes within the membrane, thus reducing penicillin-induced lethality. Possibly plays a role in programmed cell death (PCD), triggering PCD in response to penicillin, and possibly other antibiotics, and environmental stresses. | 0.979 |
