| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 |
| cidB | lytR | SAOUHSC_02850 | SAOUHSC_00231 | 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 [...] | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | 0.454 |
| cidB | lytS | SAOUHSC_02850 | SAOUHSC_00230 | 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 [...] | Two-component sensor histidine kinase, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (CAMPs). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of LytR. In turn, LytR binds to the upstream promoter regions of target genes including l [...] | 0.667 |
| hptS | lytR | SAOUHSC_00185 | SAOUHSC_00231 | Conserved hypothetical protein; Member of the two-component regulatory system HptS/HptR that regulates genes involved in hexose phosphate transport system in response to changes in extracellular phosphate sources. May act as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of HptS. In turn, HptS antagonizes CcpA-dependent transcription of a subset of CcpA-regulated genes involved in antibiotic susceptibility. | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | 0.831 |
| hptS | lytS | SAOUHSC_00185 | SAOUHSC_00230 | Conserved hypothetical protein; Member of the two-component regulatory system HptS/HptR that regulates genes involved in hexose phosphate transport system in response to changes in extracellular phosphate sources. May act as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of HptS. In turn, HptS antagonizes CcpA-dependent transcription of a subset of CcpA-regulated genes involved in antibiotic susceptibility. | Two-component sensor histidine kinase, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (CAMPs). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of LytR. In turn, LytR binds to the upstream promoter regions of target genes including l [...] | 0.404 |
| lrgA | cidB | SAOUHSC_00232 | SAOUHSC_02850 | 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. | 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 [...] | 0.979 |
| lrgA | lrgB | SAOUHSC_00232 | SAOUHSC_00233 | 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. | Holin-like protein LrgB, putative; 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. 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. | 0.994 |
| lrgA | lytR | SAOUHSC_00232 | SAOUHSC_00231 | 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. | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | 0.893 |
| lrgA | lytS | SAOUHSC_00232 | SAOUHSC_00230 | 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. | Two-component sensor histidine kinase, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (CAMPs). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of LytR. In turn, LytR binds to the upstream promoter regions of target genes including l [...] | 0.958 |
| lrgA | scdA | SAOUHSC_00232 | SAOUHSC_00229 | 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. | ScdA protein, putative; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. | 0.421 |
| lrgB | lrgA | SAOUHSC_00233 | SAOUHSC_00232 | Holin-like protein LrgB, putative; 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. 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. | 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. | 0.994 |
| lrgB | lytR | SAOUHSC_00233 | SAOUHSC_00231 | Holin-like protein LrgB, putative; 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. 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. | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | 0.951 |
| lrgB | lytS | SAOUHSC_00233 | SAOUHSC_00230 | Holin-like protein LrgB, putative; 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. 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. | Two-component sensor histidine kinase, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (CAMPs). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of LytR. In turn, LytR binds to the upstream promoter regions of target genes including l [...] | 0.922 |
| lytR | cidB | SAOUHSC_00231 | SAOUHSC_02850 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | 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 [...] | 0.454 |
| lytR | hptS | SAOUHSC_00231 | SAOUHSC_00185 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | Conserved hypothetical protein; Member of the two-component regulatory system HptS/HptR that regulates genes involved in hexose phosphate transport system in response to changes in extracellular phosphate sources. May act as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of HptS. In turn, HptS antagonizes CcpA-dependent transcription of a subset of CcpA-regulated genes involved in antibiotic susceptibility. | 0.831 |
| lytR | lrgA | SAOUHSC_00231 | SAOUHSC_00232 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | 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. | 0.893 |
| lytR | lrgB | SAOUHSC_00231 | SAOUHSC_00233 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | Holin-like protein LrgB, putative; 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. 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. | 0.951 |
| lytR | lytS | SAOUHSC_00231 | SAOUHSC_00230 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | Two-component sensor histidine kinase, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (CAMPs). Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of LytR. In turn, LytR binds to the upstream promoter regions of target genes including l [...] | 0.999 |
| lytR | msrR | SAOUHSC_00231 | SAOUHSC_01361 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | Transcriptional regulator, putative; Involved in SarA attenuation. Affects resistance to oxacillin and teicoplanin, as well as the synthesis of virulence factors. Belongs to the LytR/CpsA/Psr (LCP) family. | 0.538 |
| lytR | saeR | SAOUHSC_00231 | SAOUHSC_00715 | Two-component response regulator, putative; Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Upon phosphorylation by LytS, functions as a transcription regulator by direct binding to promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. | Response regulator, putative; Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a transcriptional regulator via a specific DNA-binding domain, recognizing motifs near the promoter sequences of target genes. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (Hla, Hlb), Coa, DNase, Spa and cell wall- associated proteins (Emp, Eap, FnbA). Acts probably downstream of the Agr system in the regulatory c [...] | 0.484 |
