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 |
| azo1658 | hslO | azo1658 | azo1657 | Putative arsenate reductase protein; 45% Arsen_reductase.IPR006504; Cons_hypoth_ArsC. Pfam:PF03960; ArsC; 1. ArsC:arsenate reductase, catalyzes the reduction of arsenate to arsenite. Probably involved in arsenic resistance; High confidence in function and specificity. | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.891 |
| azo1658 | minC | azo1658 | azo1656 | Putative arsenate reductase protein; 45% Arsen_reductase.IPR006504; Cons_hypoth_ArsC. Pfam:PF03960; ArsC; 1. ArsC:arsenate reductase, catalyzes the reduction of arsenate to arsenite. Probably involved in arsenic resistance; High confidence in function and specificity. | Putative cell division inhibitor; Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization; Belongs to the MinC family. | 0.542 |
| azo1658 | minD | azo1658 | azo1655 | Putative arsenate reductase protein; 45% Arsen_reductase.IPR006504; Cons_hypoth_ArsC. Pfam:PF03960; ArsC; 1. ArsC:arsenate reductase, catalyzes the reduction of arsenate to arsenite. Probably involved in arsenic resistance; High confidence in function and specificity. | Septum site-determining protein minD (Cell division inhibitor minD); High confidence in function and specificity. | 0.483 |
| azo1658 | minE | azo1658 | azo1654 | Putative arsenate reductase protein; 45% Arsen_reductase.IPR006504; Cons_hypoth_ArsC. Pfam:PF03960; ArsC; 1. ArsC:arsenate reductase, catalyzes the reduction of arsenate to arsenite. Probably involved in arsenic resistance; High confidence in function and specificity. | Putative cell division topological specificity factor; Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | 0.483 |
| azo1658 | tex | azo1658 | azo1659 | Putative arsenate reductase protein; 45% Arsen_reductase.IPR006504; Cons_hypoth_ArsC. Pfam:PF03960; ArsC; 1. ArsC:arsenate reductase, catalyzes the reduction of arsenate to arsenite. Probably involved in arsenic resistance; High confidence in function and specificity. | Transcription accessory protein (S1-domain containing RNA binding protein),; High confidence in function and specificity. | 0.653 |
| baf | hslO | azo0733 | azo1657 | Probable Bvg accessory factor; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family. | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.558 |
| grpE | hslO | azo1064 | azo1657 | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.670 |
| grpE | hslR | azo1064 | azo0427 | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | Heat shock protein 15 homolog (HSP15). INVOLVED IN THE RECYCLING OF FREE 50S RIBOSOMAL SUBUNITS THAT STILL CARRY A NASCENT CHAIN. BINDS RNA MORE SPECIFICALLY THAN DNA. BINDS WITH VERY HIGH AFFINITY TO THE FREE 50S RIBOSOMAL SUBUNIT. DOES NOT BIND IT WHEN IT IS PART OF THE 70S RIBOSOME; Conserved hypothetical protein. | 0.624 |
| grpE | hslU | azo1064 | azo0424 | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | ATP-dependent Hsl protease ATP-binding subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.903 |
| grpE | hslV | azo1064 | azo0423 | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.900 |
| hslO | azo1658 | azo1657 | azo1658 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Putative arsenate reductase protein; 45% Arsen_reductase.IPR006504; Cons_hypoth_ArsC. Pfam:PF03960; ArsC; 1. ArsC:arsenate reductase, catalyzes the reduction of arsenate to arsenite. Probably involved in arsenic resistance; High confidence in function and specificity. | 0.891 |
| hslO | baf | azo1657 | azo0733 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Probable Bvg accessory factor; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family. | 0.558 |
| hslO | grpE | azo1657 | azo1064 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | 0.670 |
| hslO | hslR | azo1657 | azo0427 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Heat shock protein 15 homolog (HSP15). INVOLVED IN THE RECYCLING OF FREE 50S RIBOSOMAL SUBUNITS THAT STILL CARRY A NASCENT CHAIN. BINDS RNA MORE SPECIFICALLY THAN DNA. BINDS WITH VERY HIGH AFFINITY TO THE FREE 50S RIBOSOMAL SUBUNIT. DOES NOT BIND IT WHEN IT IS PART OF THE 70S RIBOSOME; Conserved hypothetical protein. | 0.881 |
| hslO | hslU | azo1657 | azo0424 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | ATP-dependent Hsl protease ATP-binding subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.722 |
| hslO | hslV | azo1657 | azo0423 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.707 |
| hslO | minC | azo1657 | azo1656 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Putative cell division inhibitor; Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization; Belongs to the MinC family. | 0.619 |
| hslO | minD | azo1657 | azo1655 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Septum site-determining protein minD (Cell division inhibitor minD); High confidence in function and specificity. | 0.575 |
| hslO | minE | azo1657 | azo1654 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Putative cell division topological specificity factor; Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | 0.559 |
| hslO | tex | azo1657 | azo1659 | Putative 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Transcription accessory protein (S1-domain containing RNA binding protein),; High confidence in function and specificity. | 0.695 |
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