Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bhlA | cidA | BSU21420 | BSU38320 | Bacteriophage SPbeta holin-like protein; May be involved in the secretion of the autolysin BlyA. | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | 0.750 |
| bhlA | xhlB | BSU21420 | BSU12800 | Bacteriophage SPbeta holin-like protein; May be involved in the secretion of the autolysin BlyA. | Bacteriophage PBSX holin; Involved in cell lysis upon induction of PbsX; Belongs to the SPP1 holin family. | 0.758 |
| cidA | bhlA | BSU38320 | BSU21420 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Bacteriophage SPbeta holin-like protein; May be involved in the secretion of the autolysin BlyA. | 0.750 |
| cidA | cwlK | BSU38320 | BSU02810 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Murein L,D:-endopeptidase; Cleaves the linkage of the L-alanine-D-glutamic acid of B.subtilis cell wall; Belongs to the peptidase M15C family. | 0.680 |
| cidA | lrgB | BSU38320 | BSU28900 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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. | 0.941 |
| cidA | lytS | BSU38320 | BSU28930 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Two-component sensor histidine kinase [LytT]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. | 0.771 |
| cidA | lytT | BSU38320 | BSU28920 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Two-component response regulator [LytS]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. | 0.777 |
| cidA | xhlB | BSU38320 | BSU12800 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Bacteriophage PBSX holin; Involved in cell lysis upon induction of PbsX; Belongs to the SPP1 holin family. | 0.680 |
| cidA | ywbF | BSU38320 | BSU38340 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Putative sugar permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.876 |
| cidA | ywbG | BSU38320 | BSU38330 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Anti-holin factor controlling activity of murein hydrolases; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; regulator. | 0.995 |
| cidA | ywbI | BSU38320 | BSU38310 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Putative transcriptional regulator (LysR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the LysR transcriptional regulatory family. | 0.832 |
| cidA | yxaC | BSU38320 | BSU40022 | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | Putative murein hydrolase export regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.906 |
| cwlK | cidA | BSU02810 | BSU38320 | Murein L,D:-endopeptidase; Cleaves the linkage of the L-alanine-D-glutamic acid of B.subtilis cell wall; Belongs to the peptidase M15C family. | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | 0.680 |
| lrgB | cidA | BSU28900 | BSU38320 | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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 regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | 0.941 |
| lrgB | lytS | BSU28900 | BSU28930 | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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. | Two-component sensor histidine kinase [LytT]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. | 0.965 |
| lrgB | lytT | BSU28900 | BSU28920 | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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. | Two-component response regulator [LytS]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. | 0.936 |
| lrgB | ywbF | BSU28900 | BSU38340 | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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. | Putative sugar permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.685 |
| lrgB | ywbI | BSU28900 | BSU38310 | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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. | Putative transcriptional regulator (LysR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the LysR transcriptional regulatory family. | 0.481 |
| lrgB | yxaC | BSU28900 | BSU40022 | Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA 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. | Putative murein hydrolase export regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.414 |
| lytS | cidA | BSU28930 | BSU38320 | Two-component sensor histidine kinase [LytT]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. | Holin regulator of murein hydrolases; 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 CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes 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 [...] | 0.771 |
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