| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SERP2115 | cidA | SERP2115 | SERP2117 | Pyruvate oxidase; Identified by similarity to EGAD:10763; match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; Belongs to the TPP enzyme family. | LrgA family 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 hypothesized to r [...] | 0.780 |
| SERP2115 | cidB | SERP2115 | SERP2116 | Pyruvate oxidase; Identified by similarity to EGAD:10763; match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; Belongs to the TPP enzyme family. | Conserved hypothetical protein TIGR00659; 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 a [...] | 0.799 |
| SERP2115 | mgt | SERP2115 | SERP1412 | Pyruvate oxidase; Identified by similarity to EGAD:10763; match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; Belongs to the TPP enzyme family. | Transglycosylase domain protein; Peptidoglycan polymerase that catalyzes glycan chain elongation using lipid-linked disaccharide-pentapeptide as the substrate; Belongs to the glycosyltransferase 51 family. | 0.503 |
| SERP2118 | cidA | SERP2118 | SERP2117 | Transcriptional regulator, LysR family; Identified by match to protein family HMM PF00126; match to protein family HMM PF03466; Belongs to the LysR transcriptional regulatory family. | LrgA family 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 hypothesized to r [...] | 0.605 |
| SERP2118 | cidB | SERP2118 | SERP2116 | Transcriptional regulator, LysR family; Identified by match to protein family HMM PF00126; match to protein family HMM PF03466; Belongs to the LysR transcriptional regulatory family. | Conserved hypothetical protein TIGR00659; 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 a [...] | 0.514 |
| cidA | SERP2115 | SERP2117 | SERP2115 | LrgA family 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 hypothesized to r [...] | Pyruvate oxidase; Identified by similarity to EGAD:10763; match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; Belongs to the TPP enzyme family. | 0.780 |
| cidA | SERP2118 | SERP2117 | SERP2118 | LrgA family 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 hypothesized to r [...] | Transcriptional regulator, LysR family; Identified by match to protein family HMM PF00126; match to protein family HMM PF03466; Belongs to the LysR transcriptional regulatory family. | 0.605 |
| cidA | cidB | SERP2117 | SERP2116 | LrgA family 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 hypothesized to r [...] | Conserved hypothetical protein TIGR00659; 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 a [...] | 0.990 |
| cidA | lrgA | SERP2117 | SERP2026 | LrgA family 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 hypothesized to r [...] | Holin-like protein LrgA; 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. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidA/LrgA family. LrgA subfamily. | 0.744 |
| cidA | lrgB | SERP2117 | SERP2027 | LrgA family 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 hypothesized to r [...] | lrgB protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily. | 0.905 |
| cidA | mgt | SERP2117 | SERP1412 | LrgA family 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 hypothesized to r [...] | Transglycosylase domain protein; Peptidoglycan polymerase that catalyzes glycan chain elongation using lipid-linked disaccharide-pentapeptide as the substrate; Belongs to the glycosyltransferase 51 family. | 0.410 |
| cidB | SERP2115 | SERP2116 | SERP2115 | Conserved hypothetical protein TIGR00659; 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 a [...] | Pyruvate oxidase; Identified by similarity to EGAD:10763; match to protein family HMM PF00205; match to protein family HMM PF02775; match to protein family HMM PF02776; Belongs to the TPP enzyme family. | 0.799 |
| cidB | SERP2118 | SERP2116 | SERP2118 | Conserved hypothetical protein TIGR00659; 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 a [...] | Transcriptional regulator, LysR family; Identified by match to protein family HMM PF00126; match to protein family HMM PF03466; Belongs to the LysR transcriptional regulatory family. | 0.514 |
| cidB | cidA | SERP2116 | SERP2117 | Conserved hypothetical protein TIGR00659; 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 a [...] | LrgA family 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 hypothesized to r [...] | 0.990 |
| cidB | lrgA | SERP2116 | SERP2026 | Conserved hypothetical protein TIGR00659; 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 a [...] | Holin-like protein LrgA; 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. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidA/LrgA family. LrgA subfamily. | 0.983 |
| lrgA | cidA | SERP2026 | SERP2117 | Holin-like protein LrgA; 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. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidA/LrgA family. LrgA subfamily. | LrgA family 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 hypothesized to r [...] | 0.744 |
| lrgA | cidB | SERP2026 | SERP2116 | Holin-like protein LrgA; 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. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidA/LrgA family. LrgA subfamily. | Conserved hypothetical protein TIGR00659; 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 a [...] | 0.983 |
| lrgA | lrgB | SERP2026 | SERP2027 | Holin-like protein LrgA; 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. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidA/LrgA family. LrgA subfamily. | lrgB protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily. | 0.998 |
| lrgB | cidA | SERP2027 | SERP2117 | lrgB protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily. | LrgA family 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 hypothesized to r [...] | 0.905 |
| lrgB | lrgA | SERP2027 | SERP2026 | lrgB protein; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily. | Holin-like protein LrgA; 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. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidA/LrgA family. LrgA subfamily. | 0.998 |
