node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SIS50740.1 | SIS50763.1 | SAMN05421686_102117 | SAMN05421686_102118 | Putative hydrolase of the HAD superfamily. | Heat shock protein Hsp15; Belongs to the HSP15 family. | 0.844 |
SIS50740.1 | SIS50789.1 | SAMN05421686_102117 | SAMN05421686_102119 | Putative hydrolase of the HAD superfamily. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.643 |
SIS50763.1 | SIS50740.1 | SAMN05421686_102118 | SAMN05421686_102117 | Heat shock protein Hsp15; Belongs to the HSP15 family. | Putative hydrolase of the HAD superfamily. | 0.844 |
SIS50763.1 | SIS50789.1 | SAMN05421686_102118 | SAMN05421686_102119 | Heat shock protein Hsp15; Belongs to the HSP15 family. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.973 |
SIS50763.1 | dnaJ | SAMN05421686_102118 | SAMN05421686_101160 | Heat shock protein Hsp15; Belongs to the HSP15 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, [...] | 0.639 |
SIS50763.1 | grpE | SAMN05421686_102118 | SAMN05421686_101158 | Heat shock protein Hsp15; Belongs to the HSP15 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 [...] | 0.634 |
SIS50763.1 | hslU | SAMN05421686_102118 | SAMN05421686_105289 | Heat shock protein Hsp15; Belongs to the HSP15 family. | ATP-dependent HslUV 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. | 0.628 |
SIS50763.1 | hslV | SAMN05421686_102118 | SAMN05421686_105290 | Heat shock protein Hsp15; Belongs to the HSP15 family. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.732 |
SIS50763.1 | htpG | SAMN05421686_102118 | SAMN05421686_106257 | Heat shock protein Hsp15; Belongs to the HSP15 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.487 |
SIS50789.1 | SIS50740.1 | SAMN05421686_102119 | SAMN05421686_102117 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Putative hydrolase of the HAD superfamily. | 0.643 |
SIS50789.1 | SIS50763.1 | SAMN05421686_102119 | SAMN05421686_102118 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Heat shock protein Hsp15; Belongs to the HSP15 family. | 0.973 |
SIS50789.1 | coaX | SAMN05421686_102119 | SAMN05421686_1176 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | 0.575 |
SIS50789.1 | dnaJ | SAMN05421686_102119 | SAMN05421686_101160 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 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, [...] | 0.666 |
SIS50789.1 | groL | SAMN05421686_102119 | SAMN05421686_104274 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.592 |
SIS50789.1 | grpE | SAMN05421686_102119 | SAMN05421686_101158 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 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 [...] | 0.698 |
SIS50789.1 | hslU | SAMN05421686_102119 | SAMN05421686_105289 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | ATP-dependent HslUV 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. | 0.741 |
SIS50789.1 | hslV | SAMN05421686_102119 | SAMN05421686_105290 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.700 |
SIS50789.1 | htpG | SAMN05421686_102119 | SAMN05421686_106257 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.569 |
SIS50789.1 | lon | SAMN05421686_102119 | SAMN05421686_112101 | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | ATP-dependent proteinase. Serine peptidase. MEROPS family S16; 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. | 0.632 |
coaX | SIS50789.1 | SAMN05421686_1176 | SAMN05421686_102119 | Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.575 |