node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dacA | lipB | b0632 | b0630 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. Belongs to the LipB family. | 0.518 |
dacA | ybeD | b0632 | b0631 | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | UPF0250 family protein. | 0.653 |
fxsA | grpE | b4140 | b2614 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | Heat shock protein; 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 rounds of ATP-depen [...] | 0.496 |
fxsA | ibpA | b4140 | b3687 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.789 |
fxsA | ybeD | b4140 | b0631 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | UPF0250 family protein. | 0.745 |
fxsA | ybeZ | b4140 | b0660 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | Heat shock protein, putative NTPase; Putative ATP-binding protein in pho regulon; Belongs to the PhoH family. | 0.506 |
fxsA | ycjX | b4140 | b1321 | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.583 |
grpE | fxsA | b2614 | b4140 | Heat shock protein; 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 rounds of ATP-depen [...] | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | 0.496 |
grpE | ibpA | b2614 | b3687 | Heat shock protein; 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 rounds of ATP-depen [...] | Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.972 |
grpE | ybeD | b2614 | b0631 | Heat shock protein; 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 rounds of ATP-depen [...] | UPF0250 family protein. | 0.706 |
grpE | ybeZ | b2614 | b0660 | Heat shock protein; 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 rounds of ATP-depen [...] | Heat shock protein, putative NTPase; Putative ATP-binding protein in pho regulon; Belongs to the PhoH family. | 0.499 |
ibpA | fxsA | b3687 | b4140 | Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | Suppressor of F exclusion of phage T7; Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid; Belongs to the UPF0716 (FxsA) family. | 0.789 |
ibpA | grpE | b3687 | b2614 | Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | Heat shock protein; 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 rounds of ATP-depen [...] | 0.972 |
ibpA | ybeD | b3687 | b0631 | Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | UPF0250 family protein. | 0.708 |
ibpA | ycjX | b3687 | b1321 | Heat shock chaperone; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | DUF463 family protein, puatative P-loop NTPase; Putative EC 2.1 enzymes; To H.influenzae HI_1637. | 0.496 |
lipB | dacA | b0630 | b0632 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. Belongs to the LipB family. | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | 0.518 |
lipB | ybeD | b0630 | b0631 | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. Belongs to the LipB family. | UPF0250 family protein. | 0.937 |
rraB | seqA | b4255 | b0687 | Protein inhibitor of RNase E; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome; Belongs to the RraB 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 [...] | 0.764 |
rraB | ybeD | b4255 | b0631 | Protein inhibitor of RNase E; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome; Belongs to the RraB family. | UPF0250 family protein. | 0.671 |
rraB | yciS | b4255 | b1279 | Protein inhibitor of RNase E; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome; Belongs to the RraB family. | DUF1049 family inner membrane protein, function unknown; Involved in the assembly of lipopolysaccharide (LPS). Belongs to the LapA family. | 0.697 |