| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bmur_0164 | clpP | Bmur_0164 | Bmur_2019 | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.681 |
| Bmur_0164 | clpX | Bmur_0164 | Bmur_2020 | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | Sigma 54 interacting domain protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.528 |
| Bmur_0988 | clpX | Bmur_0988 | Bmur_2020 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Sigma 54 interacting domain protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.664 |
| Bmur_0988 | groL | Bmur_0988 | Bmur_0204 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.891 |
| Bmur_0988 | lon | Bmur_0988 | Bmur_1535 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.893 |
| Bmur_2018 | atpD | Bmur_2018 | Bmur_2599 | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | 0.546 |
| Bmur_2018 | clpP | Bmur_2018 | Bmur_2019 | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.850 |
| Bmur_2018 | clpX | Bmur_2018 | Bmur_2020 | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | Sigma 54 interacting domain protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.588 |
| Bmur_2018 | efp | Bmur_2018 | Bmur_2021 | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | Translation elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | 0.901 |
| Bmur_2018 | ftsH | Bmur_2018 | Bmur_1076 | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | ATP-dependent metalloprotease FtsH; 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. | 0.478 |
| Bmur_2018 | lon | Bmur_2018 | Bmur_1535 | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.460 |
| Bmur_2022 | clpX | Bmur_2022 | Bmur_2020 | KEGG: bhy:BHWA1_02224 hypothetical protein. | Sigma 54 interacting domain protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.592 |
| Bmur_2022 | efp | Bmur_2022 | Bmur_2021 | KEGG: bhy:BHWA1_02224 hypothetical protein. | Translation elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. | 0.781 |
| atpD | Bmur_2018 | Bmur_2599 | Bmur_2018 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | 0.546 |
| atpD | clpP | Bmur_2599 | Bmur_2019 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.462 |
| atpD | clpX | Bmur_2599 | Bmur_2020 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Sigma 54 interacting domain protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.755 |
| atpD | groL | Bmur_2599 | Bmur_0204 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.601 |
| atpD | lon | Bmur_2599 | Bmur_1535 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.755 |
| clpP | Bmur_0164 | Bmur_2019 | Bmur_0164 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | 0.681 |
| clpP | Bmur_2018 | Bmur_2019 | Bmur_2018 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | PFAM: trigger factor domain; KEGG: bhy:BHWA1_02220 trigger factor. | 0.850 |