| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CV_1999 | CV_2787 | CV_1999 | CV_2787 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | 0.748 |
| CV_1999 | dnaJ | CV_1999 | CV_1645 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Heat shock protein 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, [...] | 0.678 |
| CV_1999 | grpE | CV_1999 | CV_1642 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Heat shock 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- [...] | 0.864 |
| CV_1999 | hptG | CV_1999 | CV_1318 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Probable chaperone heat shock protein hptG; Molecular chaperone. Has ATPase activity. | 0.861 |
| CV_1999 | hslO | CV_1999 | CV_2000 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Heat shock protein 33, redox regulated chaperone; 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. | 0.977 |
| CV_1999 | hslU | CV_1999 | CV_0402 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Heat shock protein 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. | 0.984 |
| CV_1999 | lon | CV_1999 | CV_2555 | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | Endopeptidase 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. | 0.852 |
| CV_2787 | CV_1999 | CV_2787 | CV_1999 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | 0.748 |
| CV_2787 | dnaJ | CV_2787 | CV_1645 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Heat shock protein 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, [...] | 0.712 |
| CV_2787 | grpE | CV_2787 | CV_1642 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Heat shock 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- [...] | 0.682 |
| CV_2787 | hptG | CV_2787 | CV_1318 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Probable chaperone heat shock protein hptG; Molecular chaperone. Has ATPase activity. | 0.558 |
| CV_2787 | hslO | CV_2787 | CV_2000 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Heat shock protein 33, redox regulated chaperone; 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. | 0.889 |
| CV_2787 | hslU | CV_2787 | CV_0402 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Heat shock protein 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. | 0.728 |
| CV_2787 | hslV | CV_2787 | CV_0401 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.838 |
| CV_2787 | lon | CV_2787 | CV_2555 | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | Endopeptidase 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 |
| coaX | hslO | CV_0487 | CV_2000 | Probable transcriptional regulator, Bvg acessory factor; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family. | Heat shock protein 33, redox regulated chaperone; 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. | 0.565 |
| dnaJ | CV_1999 | CV_1645 | CV_1999 | Heat shock protein 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, [...] | Conserved hypothetical protein; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0638. | 0.678 |
| dnaJ | CV_2787 | CV_1645 | CV_2787 | Heat shock protein 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, [...] | Probable ribosome-associated heat shock protein Hsp15; Identified by sequence similarity; putative; ORF located using GeneMark/Blastx/COG1188. | 0.712 |
| dnaJ | grpE | CV_1645 | CV_1642 | Heat shock protein 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, [...] | Heat shock 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- [...] | 0.995 |
| dnaJ | hptG | CV_1645 | CV_1318 | Heat shock protein 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, [...] | Probable chaperone heat shock protein hptG; Molecular chaperone. Has ATPase activity. | 0.996 |
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