node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFB67263.1 | SFB71294.1 | SAMN02745150_00041 | SAMN02745150_00415 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | Flagellar motor switch protein FliN/FliY; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | 0.601 |
SFB67263.1 | clpP | SAMN02745150_00041 | SAMN02745150_00747 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB 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. | 0.967 |
SFB67263.1 | dnaJ | SAMN02745150_00041 | SAMN02745150_00701 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | 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, [...] | 0.872 |
SFB67263.1 | dnaK | SAMN02745150_00041 | SAMN02745150_00702 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.985 |
SFB67263.1 | groL | SAMN02745150_00041 | SAMN02745150_00099 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.708 |
SFB67263.1 | groS | SAMN02745150_00041 | SAMN02745150_00898 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.710 |
SFB67263.1 | grpE | SAMN02745150_00041 | SAMN02745150_00703 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | 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 [...] | 0.865 |
SFB67263.1 | topA | SAMN02745150_00041 | SAMN02745150_00101 | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | DNA topoisomerase-1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.492 |
SFB71294.1 | SFB67263.1 | SAMN02745150_00415 | SAMN02745150_00041 | Flagellar motor switch protein FliN/FliY; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | 0.601 |
SFB71294.1 | groL | SAMN02745150_00415 | SAMN02745150_00099 | Flagellar motor switch protein FliN/FliY; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.905 |
SFB71294.1 | grpE | SAMN02745150_00415 | SAMN02745150_00703 | Flagellar motor switch protein FliN/FliY; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | 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 [...] | 0.533 |
SFB82976.1 | groL | SAMN02745150_00983 | SAMN02745150_00099 | Glucose-1-phosphate adenylyltransferase; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.830 |
SFB87664.1 | clpP | SAMN02745150_01153 | SAMN02745150_00747 | Thioredoxin; Belongs to the thioredoxin 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. | 0.564 |
SFB87664.1 | dnaJ | SAMN02745150_01153 | SAMN02745150_00701 | Thioredoxin; Belongs to the thioredoxin family. | 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, [...] | 0.548 |
SFB87664.1 | dnaK | SAMN02745150_01153 | SAMN02745150_00702 | Thioredoxin; Belongs to the thioredoxin family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.552 |
SFB87664.1 | groL | SAMN02745150_01153 | SAMN02745150_00099 | Thioredoxin; Belongs to the thioredoxin family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.905 |
SFB87664.1 | groS | SAMN02745150_01153 | SAMN02745150_00898 | Thioredoxin; Belongs to the thioredoxin family. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.672 |
SFB87664.1 | grpE | SAMN02745150_01153 | SAMN02745150_00703 | Thioredoxin; Belongs to the thioredoxin family. | 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 [...] | 0.636 |
SFB87664.1 | topA | SAMN02745150_01153 | SAMN02745150_00101 | Thioredoxin; Belongs to the thioredoxin family. | DNA topoisomerase-1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.514 |
clpP | SFB67263.1 | SAMN02745150_00747 | SAMN02745150_00041 | 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. | ATP-dependent Clp protease ATP-binding subunit ClpB; Belongs to the ClpA/ClpB family. | 0.967 |