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 |
| argA | bamA | b2818 | b0177 | Amino acid n-acetyltransferase and inactive acetylglutamate kinase; Belongs to the acetyltransferase family. ArgA subfamily | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | 0.449 |
| argA | bepA | b2818 | b2494 | Amino acid n-acetyltransferase and inactive acetylglutamate kinase; Belongs to the acetyltransferase family. ArgA subfamily | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | 0.571 |
| bamA | argA | b0177 | b2818 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | Amino acid n-acetyltransferase and inactive acetylglutamate kinase; Belongs to the acetyltransferase family. ArgA subfamily | 0.449 |
| bamA | bepA | b0177 | b2494 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | 0.593 |
| bamA | lptD | b0177 | b0054 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | Lps assembly om complex lptde, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance | 0.992 |
| bamA | surA | b0177 | b0053 | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | Peptidyl-prolyl cis-trans isomerase (ppiase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis | 0.999 |
| bepA | argA | b2494 | b2818 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Amino acid n-acetyltransferase and inactive acetylglutamate kinase; Belongs to the acetyltransferase family. ArgA subfamily | 0.571 |
| bepA | bamA | b2494 | b0177 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | 0.593 |
| bepA | lptD | b2494 | b0054 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Lps assembly om complex lptde, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance | 0.604 |
| bepA | surA | b2494 | b0053 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Peptidyl-prolyl cis-trans isomerase (ppiase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis | 0.675 |
| bepA | ycaL | b2494 | b0909 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process | 0.866 |
| bepA | ydgD | b2494 | b1598 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Putative serine protease ydgd; Belongs to the peptidase S1B family | 0.601 |
| bepA | yecR | b2494 | b1904 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | annotation not available | 0.578 |
| bepA | yfgD | b2494 | b2495 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Arsenate reductase (glutaredoxin); Belongs to the ArsC family | 0.860 |
| bepA | yfgI | b2494 | b2506 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Nalidixic acid resistance protein, putative periplasmic protein; Uncharacterized protein YfgI; Putative membrane protein | 0.734 |
| bepA | yfgO | b2494 | b2493 | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | Putative upf0118 family inner membrane permease; Putative permease | 0.740 |
| lptD | bamA | b0054 | b0177 | Lps assembly om complex lptde, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | 0.992 |
| lptD | bepA | b0054 | b2494 | Lps assembly om complex lptde, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance | Om protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions | 0.604 |
| lptD | surA | b0054 | b0053 | Lps assembly om complex lptde, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance | Peptidyl-prolyl cis-trans isomerase (ppiase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis | 0.995 |
| surA | bamA | b0053 | b0177 | Peptidyl-prolyl cis-trans isomerase (ppiase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis | Bamabcde complex om biogenesis outer membrane pore-forming assembly factor; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. 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 complete Bam [...] | 0.999 |
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