| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SGO_1993 | gshAB | SGO_1993 | SGO_1990 | Possible transcriptional regulator; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | Glutamate--cysteine ligase, putative/amino acid ligase, putative; Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine; In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily. | 0.660 |
| SGO_1993 | hslO | SGO_1993 | SGO_1991 | Possible transcriptional regulator; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. | 33 kDa chaperonin /Heat shock protein 33-like protein; 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. | 0.810 |
| SGO_2139 | grpE | SGO_2139 | SGO_0401 | S4 RNA-binding domain protein; Identified by match to protein family HMM PF01479. | Co-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-depend [...] | 0.519 |
| SGO_2139 | hslO | SGO_2139 | SGO_1991 | S4 RNA-binding domain protein; Identified by match to protein family HMM PF01479. | 33 kDa chaperonin /Heat shock protein 33-like protein; 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. | 0.787 |
| dnaK | groES | SGO_0402 | SGO_1886 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.978 |
| dnaK | groL | SGO_0402 | SGO_1885 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin/groEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.989 |
| dnaK | grpE | SGO_0402 | SGO_0401 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-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-depend [...] | 0.999 |
| dnaK | gshAB | SGO_0402 | SGO_1990 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Glutamate--cysteine ligase, putative/amino acid ligase, putative; Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine; In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily. | 0.440 |
| dnaK | hslO | SGO_0402 | SGO_1991 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 33 kDa chaperonin /Heat shock protein 33-like protein; 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. | 0.618 |
| dnaK | msrA | SGO_0402 | SGO_0278 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Peptide methionine sulfoxide reductase msrA/msrB; 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 (By similarity). Involved in protection against oxidative stress when the bacterium enters the host bloodstream and required for maximal growth under aerobic and anaerobic conditions. | 0.454 |
| dnaK | msrA-2 | SGO_0402 | SGO_1176 | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Peptide methionine sulfoxide reductase-like protein; 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. | 0.454 |
| groES | dnaK | SGO_1886 | SGO_0402 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
| groES | groL | SGO_1886 | SGO_1885 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 60 kDa chaperonin/groEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| groES | grpE | SGO_1886 | SGO_0401 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Co-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-depend [...] | 0.965 |
| groES | hslO | SGO_1886 | SGO_1991 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 33 kDa chaperonin /Heat shock protein 33-like protein; 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. | 0.652 |
| groES | msrA | SGO_1886 | SGO_0278 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Peptide methionine sulfoxide reductase msrA/msrB; 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 (By similarity). Involved in protection against oxidative stress when the bacterium enters the host bloodstream and required for maximal growth under aerobic and anaerobic conditions. | 0.620 |
| groES | msrA-2 | SGO_1886 | SGO_1176 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Peptide methionine sulfoxide reductase-like protein; 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. | 0.620 |
| groES | trxB | SGO_1886 | SGO_0581 | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Thioredoxin-disulfide reductase; Identified by match to protein family HMM PF00070; match to protein family HMM PF01134; match to protein family HMM PF01266; match to protein family HMM PF03486; match to protein family HMM PF07992; match to protein family HMM TIGR01292. | 0.431 |
| groL | dnaK | SGO_1885 | SGO_0402 | 60 kDa chaperonin/groEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | DnaK chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.989 |
| groL | groES | SGO_1885 | SGO_1886 | 60 kDa chaperonin/groEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
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