| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEM79637.1 | clpP | Thewi_2289 | Thewi_0740 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit; 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. | 0.967 |
| AEM79637.1 | clpX | Thewi_2289 | Thewi_0741 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.545 |
| AEM79637.1 | groL | Thewi_2289 | Thewi_0664 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.710 |
| AEM79637.1 | grpE | Thewi_2289 | Thewi_1042 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | Protein 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 i [...] | 0.906 |
| AEM79637.1 | hslU | Thewi_2289 | Thewi_1402 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | ATPase AAA-2 domain protein; 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. | 0.724 |
| AEM79637.1 | hslV | Thewi_2289 | Thewi_1403 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.620 |
| AEM79637.1 | lon | Thewi_2289 | Thewi_0742 | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | Anti-sigma H sporulation factor, LonB; 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. | 0.824 |
| atpA | atpH | Thewi_0749 | Thewi_0748 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.999 |
| atpA | clpP | Thewi_0749 | Thewi_0740 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP-dependent Clp protease proteolytic subunit; 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. | 0.530 |
| atpA | clpX | Thewi_0749 | Thewi_0741 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.610 |
| atpA | groL | Thewi_0749 | Thewi_0664 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.675 |
| atpA | lon | Thewi_0749 | Thewi_0742 | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Anti-sigma H sporulation factor, LonB; 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. | 0.817 |
| atpH | atpA | Thewi_0748 | Thewi_0749 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.999 |
| atpH | engB | Thewi_0748 | Thewi_0743 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | GTP-binding protein engB; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.429 |
| atpH | lon | Thewi_0748 | Thewi_0742 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Anti-sigma H sporulation factor, LonB; 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. | 0.813 |
| clpP | AEM79637.1 | Thewi_0740 | Thewi_2289 | ATP-dependent Clp protease proteolytic subunit; 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. | KEGG: tbo:Thebr_0352 ATPase AAA-2 domain-containing protein; PFAM: ATPase associated with various cellular activities, AAA-2; Clp, N-terminal; ATPase, AAA-type, core; UvrB/UvrC protein; Clp ATPase, C-terminal; SMART: ATPase, AAA+ type, core; Belongs to the ClpA/ClpB family. | 0.967 |
| clpP | atpA | Thewi_0740 | Thewi_0749 | ATP-dependent Clp protease proteolytic subunit; 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. | ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.530 |
| clpP | clpX | Thewi_0740 | Thewi_0741 | ATP-dependent Clp protease proteolytic subunit; 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. | ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.996 |
| clpP | engB | Thewi_0740 | Thewi_0743 | ATP-dependent Clp protease proteolytic subunit; 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. | GTP-binding protein engB; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.605 |
| clpP | groL | Thewi_0740 | Thewi_0664 | ATP-dependent Clp protease proteolytic subunit; 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. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.781 |
