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 |
| aroC | epmC | b2329 | b2326 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. | Elongation Factor P Lys34 hydroxylase; Is involved in the final hydroxylation step of the post- translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine. | 0.800 |
| aroC | mepA | b2329 | b2328 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. | Murein DD-endopeptidase; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. | 0.932 |
| aroC | yfcA | b2329 | b2327 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. | TauE/TSUP family inner membrane protein; Putative structural protein. | 0.809 |
| aroC | yfcL | b2329 | b2325 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. | Uncharacterized protein. | 0.712 |
| bamC | lptC | b2477 | b3199 | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | 0.778 |
| bamC | seqA | b2477 | b0687 | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | Negative modulator of initiation of replication; Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re- initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. Can also bind to hemimethylated GATC sequences outside of oriC region. Binds, with less affinity, to fully methylated GATC si [...] | 0.783 |
| bamC | yejL | b2477 | b2187 | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | UPF0352 family protein; Belongs to the UPF0352 family. | 0.714 |
| bamC | yfcL | b2477 | b2325 | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | Uncharacterized protein. | 0.734 |
| bamC | yheV | b2477 | b4551 | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | DUF2387 family putative metal-binding protein. | 0.477 |
| bamC | zapC | b2477 | b0946 | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | FtsZ stabilizer; Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. | 0.744 |
| epmC | aroC | b2326 | b2329 | Elongation Factor P Lys34 hydroxylase; Is involved in the final hydroxylation step of the post- translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine. | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. | 0.800 |
| epmC | mepA | b2326 | b2328 | Elongation Factor P Lys34 hydroxylase; Is involved in the final hydroxylation step of the post- translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine. | Murein DD-endopeptidase; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. | 0.806 |
| epmC | yfcA | b2326 | b2327 | Elongation Factor P Lys34 hydroxylase; Is involved in the final hydroxylation step of the post- translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine. | TauE/TSUP family inner membrane protein; Putative structural protein. | 0.973 |
| epmC | yfcL | b2326 | b2325 | Elongation Factor P Lys34 hydroxylase; Is involved in the final hydroxylation step of the post- translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and does not modify the added beta-lysine. | Uncharacterized protein. | 0.921 |
| lptC | bamC | b3199 | b2477 | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | BamABCDE complex OM biogenesis lipoprotein; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly [...] | 0.778 |
| lptC | seqA | b3199 | b0687 | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | Negative modulator of initiation of replication; Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re- initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. Can also bind to hemimethylated GATC sequences outside of oriC region. Binds, with less affinity, to fully methylated GATC si [...] | 0.773 |
| lptC | yejL | b3199 | b2187 | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | UPF0352 family protein; Belongs to the UPF0352 family. | 0.776 |
| lptC | yfcL | b3199 | b2325 | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | Uncharacterized protein. | 0.729 |
| lptC | yheV | b3199 | b4551 | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | DUF2387 family putative metal-binding protein. | 0.657 |
| lptC | zapC | b3199 | b0946 | Periplasmic membrane-anchored LPS-binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | FtsZ stabilizer; Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. | 0.751 |
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