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 |
| degS | ompA | STM3349 | STM1070 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.680 |
| degS | rseA | STM3349 | STM2639 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Anti sigma E (sigma 24) factor, negative regulator; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytop [...] | 0.986 |
| fliC | fljB | STM1959 | STM2771 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.989 |
| fliC | ftsZ | STM1959 | STM0133 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.441 |
| fliC | htrA | STM1959 | STM0209 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | 0.611 |
| fliC | ompA | STM1959 | STM1070 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.915 |
| fliC | rseA | STM1959 | STM2639 | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Anti sigma E (sigma 24) factor, negative regulator; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytop [...] | 0.809 |
| fljB | fliC | STM2771 | STM1959 | Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.989 |
| fljB | htrA | STM2771 | STM0209 | Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | 0.499 |
| fljB | ompA | STM2771 | STM1070 | Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.815 |
| fljB | rseA | STM2771 | STM2639 | Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Anti sigma E (sigma 24) factor, negative regulator; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytop [...] | 0.576 |
| ftsX | ftsZ | STM3569 | STM0133 | Putative integral membrane cell division protein; Part of the ABC transporter FtsEX involved in cellular division; Belongs to the ABC-4 integral membrane protein family. FtsX subfamily. | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.838 |
| ftsX | mrcB | STM3569 | STM0190 | Putative integral membrane cell division protein; Part of the ABC transporter FtsEX involved in cellular division; Belongs to the ABC-4 integral membrane protein family. FtsX subfamily. | Transpeptidase of penicillin-binding protein 1b; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.578 |
| ftsZ | fliC | STM0133 | STM1959 | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.441 |
| ftsZ | ftsX | STM0133 | STM3569 | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Putative integral membrane cell division protein; Part of the ABC transporter FtsEX involved in cellular division; Belongs to the ABC-4 integral membrane protein family. FtsX subfamily. | 0.838 |
| ftsZ | mrcB | STM0133 | STM0190 | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Transpeptidase of penicillin-binding protein 1b; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). | 0.868 |
| ftsZ | ompA | STM0133 | STM1070 | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Putative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. | 0.680 |
| ftsZ | yafK | STM0133 | STM0312 | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | Putative periplasmic protein; Similar to E. coli orf, hypothetical protein (AAC73328.1); Blastp hit to AAC73328.1 (246 aa), 90% identity in aa 1 - 246. | 0.762 |
| htrA | fliC | STM0209 | STM1959 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.611 |
| htrA | fljB | STM0209 | STM2771 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Filament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.499 |
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