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 protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ccpA | fbaA | BSU29740 | BSU37120 | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. | Fructose-1,6-bisphosphate aldolase; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. | 0.737 |
| ccpA | ykwC | BSU29740 | BSU13960 | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.570 |
| ctaF | ykwC | BSU14920 | BSU13960 | Cytochrome caa3 oxidase (subunit IV); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase bacterial subunit 4 family. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.524 |
| fbaA | ccpA | BSU37120 | BSU29740 | Fructose-1,6-bisphosphate aldolase; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. | 0.737 |
| fbaA | ykwC | BSU37120 | BSU13960 | Fructose-1,6-bisphosphate aldolase; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.871 |
| iolJ | mmsA | BSU39670 | BSU39760 | 2-deoxy-5-keto-D-gluconic acid 6-phosphate aldolase; Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6- phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily. | Methylmalonate-semialdehyde dehydrogenase; Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. | 0.992 |
| iolJ | ykwC | BSU39670 | BSU13960 | 2-deoxy-5-keto-D-gluconic acid 6-phosphate aldolase; Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6- phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.860 |
| mmsA | iolJ | BSU39760 | BSU39670 | Methylmalonate-semialdehyde dehydrogenase; Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. | 2-deoxy-5-keto-D-gluconic acid 6-phosphate aldolase; Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6- phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily. | 0.992 |
| mmsA | ykwC | BSU39760 | BSU13960 | Methylmalonate-semialdehyde dehydrogenase; Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.573 |
| prkC | prpC | BSU15770 | BSU15760 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | 0.999 |
| prkC | yabT | BSU15770 | BSU00660 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.966 |
| prkC | ykwC | BSU15770 | BSU13960 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.756 |
| prkC | ymfM | BSU15770 | BSU16910 | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | Conserved hypothetical protein with ACT domain; Evidence 7: Gene remnant. | 0.573 |
| prpC | prkC | BSU15760 | BSU15770 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | 0.999 |
| prpC | yabT | BSU15760 | BSU00660 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | 0.816 |
| prpC | ykwC | BSU15760 | BSU13960 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.685 |
| prpC | ymfM | BSU15760 | BSU16910 | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | Conserved hypothetical protein with ACT domain; Evidence 7: Gene remnant. | 0.504 |
| yabT | prkC | BSU00660 | BSU15770 | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...] | 0.966 |
| yabT | prpC | BSU00660 | BSU15760 | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB. | 0.816 |
| yabT | ykwC | BSU00660 | BSU13960 | Putative serine/threonine-protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. | Putative beta-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the HIBADH-related family. | 0.714 |
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