node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cutA | cutC | b4137 | b1874 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Copper homeostasis protein; Participates in the control of copper homeostasis. Belongs to the CutC family. | 0.782 |
cutA | dsbC | b4137 | b2893 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.898 |
cutA | dsbD | b4137 | b4136 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. | 0.985 |
cutA | fxsA | b4137 | b4140 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | 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. | 0.597 |
cutA | groL | b4137 | b4143 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.763 |
cutA | groS | b4137 | b4142 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.881 |
cutA | lnt | b4137 | b0657 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...] | 0.681 |
cutA | nlpE | b4137 | b0192 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Lipoprotein involved with copper homeostasis and adhesion; Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR. DegP induction seems to require membrane anchoring of this protein. Structural changes and/or interaction of the CXXC m [...] | 0.687 |
cutA | trpC | b4137 | b1262 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | Indole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase; Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. | 0.922 |
cutA | yjdC | b4137 | b4135 | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | tRNA-Phe; Anticodon: GAA. | 0.853 |
cutC | cutA | b1874 | b4137 | Copper homeostasis protein; Participates in the control of copper homeostasis. Belongs to the CutC family. | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | 0.782 |
cutC | lnt | b1874 | b0657 | Copper homeostasis protein; Participates in the control of copper homeostasis. Belongs to the CutC family. | Apolipoprotein N-acyltransferase; Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. Utilizes a two-step reaction via a ping-pong mechanism. Lnt undergoes covalent modification in the presence of phospholipids, resulting in a thioester acyl-enzyme intermediate. It then transfers the acyl chain to the amine group of the N-terminal diacylglyceryl-modified cysteine of apolipoprotein, leading to the formation of mature triacylated lipoprotein. In vitro, can utilize the phospholipids phosphatidylethanolami [...] | 0.533 |
cutC | nlpE | b1874 | b0192 | Copper homeostasis protein; Participates in the control of copper homeostasis. Belongs to the CutC family. | Lipoprotein involved with copper homeostasis and adhesion; Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes. Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation. Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR. DegP induction seems to require membrane anchoring of this protein. Structural changes and/or interaction of the CXXC m [...] | 0.704 |
dsbC | cutA | b2893 | b4137 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | 0.898 |
dsbC | dsbD | b2893 | b4136 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. | 0.999 |
dsbC | groL | b2893 | b4143 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.733 |
dsbC | groS | b2893 | b4142 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.674 |
dsbC | trpC | b2893 | b1262 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Indole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase; Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. | 0.921 |
dsbD | cutA | b4136 | b4137 | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. | Divalent-cation tolerance protein, copper sensitivity; Involved in resistance toward heavy metals. Belongs to the CutA family. | 0.985 |
dsbD | dsbC | b4136 | b2893 | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.999 |