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 |
| ftsI | ftsI-2 | STM0122 | STM1836 | Division specific transpeptidase; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | Putative penicillin-binding protein-3; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | 0.901 |
| ftsI | prc | STM0122 | STM1845 | Division specific transpeptidase; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 0.706 |
| ftsI-2 | ftsI | STM1836 | STM0122 | Putative penicillin-binding protein-3; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | Division specific transpeptidase; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | 0.901 |
| ftsI-2 | prc | STM1836 | STM1845 | Putative penicillin-binding protein-3; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 0.696 |
| htrA | nlpI | STM0209 | STM3281 | 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 [...] | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | 0.415 |
| htrA | prc | STM0209 | STM1845 | 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 [...] | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 0.543 |
| htrA | yaeL | STM0209 | STM0223 | 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 [...] | Putative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. | 0.833 |
| nifJ | prc | STM1651 | STM1845 | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 0.679 |
| nlpI | htrA | STM3281 | STM0209 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | 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 [...] | 0.415 |
| nlpI | prc | STM3281 | STM1845 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 0.955 |
| nlpI | proQ | STM3281 | STM1846 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | Activator of proP; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. Belongs to the ProQ family. | 0.858 |
| pheS | prc | STM1337 | STM1845 | Similar to E. coli phenylalanine tRNA synthetase, alpha-subunit (AAC74784.1); Blastp hit to AAC74784.1 (327 aa), 97% identity in aa 1 - 327. | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 0.563 |
| prc | ftsI | STM1845 | STM0122 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Division specific transpeptidase; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | 0.706 |
| prc | ftsI-2 | STM1845 | STM1836 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Putative penicillin-binding protein-3; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. | 0.696 |
| prc | htrA | STM1845 | STM0209 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | 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 [...] | 0.543 |
| prc | nifJ | STM1845 | STM1651 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Similar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. | 0.679 |
| prc | nlpI | STM1845 | STM3281 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | 0.955 |
| prc | pheS | STM1845 | STM1337 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Similar to E. coli phenylalanine tRNA synthetase, alpha-subunit (AAC74784.1); Blastp hit to AAC74784.1 (327 aa), 97% identity in aa 1 - 327. | 0.563 |
| prc | proQ | STM1845 | STM1846 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Activator of proP; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. Belongs to the ProQ family. | 0.935 |
| prc | yaeL | STM1845 | STM0223 | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). | Putative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. | 0.681 |
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