| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| argB | argD | HRM2_27580 | HRM2_27570 | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | 0.991 |
| argB | argF | HRM2_27580 | HRM2_27560 | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | 0.982 |
| argB | hslU | HRM2_27580 | HRM2_27590 | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | HslU; 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. | 0.820 |
| argB | hslV | HRM2_27580 | HRM2_27600 | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.820 |
| argB | xerC-2 | HRM2_27580 | HRM2_27610 | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | Site-specific recombinase XerD (DNA replication, recombination and repair); Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.780 |
| argD | argB | HRM2_27570 | HRM2_27580 | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | 0.991 |
| argD | argF | HRM2_27570 | HRM2_27560 | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | 0.982 |
| argD | hslU | HRM2_27570 | HRM2_27590 | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | HslU; 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. | 0.811 |
| argD | hslV | HRM2_27570 | HRM2_27600 | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.809 |
| argD | xerC-2 | HRM2_27570 | HRM2_27610 | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | Site-specific recombinase XerD (DNA replication, recombination and repair); Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.768 |
| argF | argB | HRM2_27560 | HRM2_27580 | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | ArgB; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | 0.982 |
| argF | argD | HRM2_27560 | HRM2_27570 | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | ArgD; Acetylornithine/succinyldiaminopimelate aminotransferase ArgD (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. | 0.982 |
| argF | hslU | HRM2_27560 | HRM2_27590 | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | HslU; 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. | 0.814 |
| argF | hslV | HRM2_27560 | HRM2_27600 | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.791 |
| argF | xerC-2 | HRM2_27560 | HRM2_27610 | ArgF; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | Site-specific recombinase XerD (DNA replication, recombination and repair); Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.754 |
| dnaJ2 | groEL | HRM2_11430 | HRM2_30600 | DnaJ2; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are [...] | GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.927 |
| dnaJ2 | groES | HRM2_11430 | HRM2_30610 | DnaJ2; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are [...] | GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.848 |
| dnaJ2 | grpE | HRM2_11430 | HRM2_04040 | DnaJ2; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are [...] | 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 rounds of ATP-dependent interacti [...] | 0.979 |
| dnaJ2 | hslU | HRM2_11430 | HRM2_27590 | DnaJ2; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are [...] | HslU; 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. | 0.920 |
| dnaJ2 | hslV | HRM2_11430 | HRM2_27600 | DnaJ2; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, DnaK and GrpE are [...] | HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.896 |
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