| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMG70918.1 | dnaJ | AL531_11480 | AL531_17860 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; 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, [...] | 0.765 |
| AMG70918.1 | grpE | AL531_11480 | AL531_03400 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 [...] | 0.908 |
| AMG70918.1 | hslU | AL531_11480 | AL531_16280 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit 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. | 0.906 |
| AMG70918.1 | htpX | AL531_11480 | AL531_08075 | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | Zinc metalloprotease HtpX; Metalloprotease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.592 |
| dnaJ | AMG70918.1 | AL531_17860 | AL531_11480 | Molecular chaperone DnaJ; 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, [...] | Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.765 |
| dnaJ | grpE | AL531_17860 | AL531_03400 | Molecular chaperone DnaJ; 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, [...] | Molecular chaperone 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 [...] | 0.987 |
| dnaJ | hflB | AL531_17860 | AL531_14125 | Molecular chaperone DnaJ; 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, [...] | ATP-dependent metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.782 |
| dnaJ | hslU | AL531_17860 | AL531_16280 | Molecular chaperone DnaJ; 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, [...] | ATP-dependent protease ATP-binding subunit 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. | 0.962 |
| dnaJ | htpX | AL531_17860 | AL531_08075 | Molecular chaperone DnaJ; 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, [...] | Zinc metalloprotease HtpX; Metalloprotease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.574 |
| dnaJ | rrmJ | AL531_17860 | AL531_14130 | Molecular chaperone DnaJ; 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, [...] | 23S rRNA methyltransferase; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. | 0.613 |
| fadB | ftsE | AL531_17460 | AL531_12790 | Multifunctional fatty acid oxidation complex subunit alpha; Splits dipeptides with a prolyl residue in the C-terminal position. | Cell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. | 0.576 |
| fadB | htpX | AL531_17460 | AL531_08075 | Multifunctional fatty acid oxidation complex subunit alpha; Splits dipeptides with a prolyl residue in the C-terminal position. | Zinc metalloprotease HtpX; Metalloprotease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.639 |
| fadB | htrB_3 | AL531_17460 | AL531_04115 | Multifunctional fatty acid oxidation complex subunit alpha; Splits dipeptides with a prolyl residue in the C-terminal position. | Lipid A biosynthesis lauroyl acyltransferase; Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A). | 0.563 |
| fadB | pcnB | AL531_17460 | AL531_00740 | Multifunctional fatty acid oxidation complex subunit alpha; Splits dipeptides with a prolyl residue in the C-terminal position. | poly(A) polymerase I; Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | 0.571 |
| fadB | rrmJ | AL531_17460 | AL531_14130 | Multifunctional fatty acid oxidation complex subunit alpha; Splits dipeptides with a prolyl residue in the C-terminal position. | 23S rRNA methyltransferase; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. | 0.558 |
| ftsE | fadB | AL531_12790 | AL531_17460 | Cell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. | Multifunctional fatty acid oxidation complex subunit alpha; Splits dipeptides with a prolyl residue in the C-terminal position. | 0.576 |
| ftsE | hflB | AL531_12790 | AL531_14125 | Cell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. | ATP-dependent metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.427 |
| ftsE | htpX | AL531_12790 | AL531_08075 | Cell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. | Zinc metalloprotease HtpX; Metalloprotease; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.572 |
| ftsE | htrB_3 | AL531_12790 | AL531_04115 | Cell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. | Lipid A biosynthesis lauroyl acyltransferase; Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A). | 0.572 |
| ftsE | pcnB | AL531_12790 | AL531_00740 | Cell division ATP-binding protein FtsE; Part of the ABC transporter FtsEX involved in cellular division. | poly(A) polymerase I; Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | 0.571 |
