node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SHJ43683.1 | hslO | SAMN02745248_00110 | SAMN02745248_02092 | 16S rRNA (cytosine967-C5)-methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 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. | 0.525 |
SHJ43683.1 | lysS | SAMN02745248_00110 | SAMN02745248_00941 | 16S rRNA (cytosine967-C5)-methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.933 |
SHJ80160.1 | SHK45017.1 | SAMN02745248_00960 | SAMN02745248_02563 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | Molecular chaperone HtpG. | 0.491 |
SHJ80160.1 | grpE | SAMN02745248_00960 | SAMN02745248_00191 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | 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 [...] | 0.565 |
SHJ80160.1 | hslO | SAMN02745248_00960 | SAMN02745248_02092 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | 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. | 0.852 |
SHK22828.1 | SHK22848.1 | SAMN02745248_02090 | SAMN02745248_02091 | Small, acid-soluble spore protein, alpha/beta type. | Methyltransferase domain-containing protein. | 0.736 |
SHK22828.1 | hslO | SAMN02745248_02090 | SAMN02745248_02092 | Small, acid-soluble spore protein, alpha/beta type. | 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. | 0.744 |
SHK22848.1 | SHK22828.1 | SAMN02745248_02091 | SAMN02745248_02090 | Methyltransferase domain-containing protein. | Small, acid-soluble spore protein, alpha/beta type. | 0.736 |
SHK22848.1 | hslO | SAMN02745248_02091 | SAMN02745248_02092 | Methyltransferase domain-containing protein. | 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. | 0.872 |
SHK45017.1 | SHJ80160.1 | SAMN02745248_02563 | SAMN02745248_00960 | Molecular chaperone HtpG. | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | 0.491 |
SHK45017.1 | groL | SAMN02745248_02563 | SAMN02745248_00443 | Molecular chaperone HtpG. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.967 |
SHK45017.1 | grpE | SAMN02745248_02563 | SAMN02745248_00191 | Molecular chaperone HtpG. | 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 [...] | 0.923 |
SHK45017.1 | hslO | SAMN02745248_02563 | SAMN02745248_02092 | Molecular chaperone HtpG. | 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. | 0.581 |
SHK45017.1 | lon | SAMN02745248_02563 | SAMN02745248_01920 | Molecular chaperone HtpG. | ATP-dependent Lon protease; 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. | 0.812 |
groL | SHK45017.1 | SAMN02745248_00443 | SAMN02745248_02563 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone HtpG. | 0.967 |
groL | grpE | SAMN02745248_00443 | SAMN02745248_00191 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.992 |
groL | hslO | SAMN02745248_00443 | SAMN02745248_02092 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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. | 0.716 |
groL | lon | SAMN02745248_00443 | SAMN02745248_01920 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent Lon protease; 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. | 0.841 |
groL | lysS | SAMN02745248_00443 | SAMN02745248_00941 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.460 |
groL | msrA | SAMN02745248_00443 | SAMN02745248_01617 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Peptide-methionine (S)-S-oxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.748 |