node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABD29370.1 | hly | SAOUHSC_00192 | SAOUHSC_01121 | Coagulase. | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.433 |
ABD30228.1 | ebpS | SAOUHSC_01114 | SAOUHSC_01501 | Fibrinogen-binding protein. | Elastin binding protein; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect. | 0.708 |
ABD30228.1 | hly | SAOUHSC_01114 | SAOUHSC_01121 | Fibrinogen-binding protein. | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.529 |
agrB | ebpS | SAOUHSC_02261 | SAOUHSC_01501 | Accessory gene regulator protein B; Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP; Belongs to the AgrB family. | Elastin binding protein; Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). May be involved in sensing the environment or in nutrient transport, since its loss caused a growth defect. | 0.646 |
agrB | hly | SAOUHSC_02261 | SAOUHSC_01121 | Accessory gene regulator protein B; Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP; Belongs to the AgrB family. | Alpha-hemolysin precursor; Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Inhibits host neutrophil chemotaxis to the lesion region (Probable). Heptamer oligomerization and pore formation is required for lytic activity (By similarity). Belongs to the aerolysin family. | 0.594 |
agrB | srtA | SAOUHSC_02261 | SAOUHSC_02834 | Accessory gene regulator protein B; Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP; Belongs to the AgrB family. | Sortase, putative; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the disp [...] | 0.512 |
ahpC | clpB | SAOUHSC_00365 | SAOUHSC_00912 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.428 |
ahpC | clpC | SAOUHSC_00365 | SAOUHSC_00505 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | 0.432 |
ahpC | dnaK | SAOUHSC_00365 | SAOUHSC_01683 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | DNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.802 |
ahpC | groL | SAOUHSC_00365 | SAOUHSC_02254 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | Chaperonin, 60 kDa, GrpEL, putative; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.674 |
ahpC | groS | SAOUHSC_00365 | SAOUHSC_02255 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | Chaperonin, 10 kDa, GroES, putative; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.555 |
ahpC | grpE | SAOUHSC_00365 | SAOUHSC_01684 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | 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 [...] | 0.636 |
ahpC | tpiA | SAOUHSC_00365 | SAOUHSC_00797 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. | 0.471 |
clpB | ahpC | SAOUHSC_00912 | SAOUHSC_00365 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is important for survival under desiccation conditions. Not required for virulence although is necessary for nasal colonization. | 0.428 |
clpB | clpX | SAOUHSC_00912 | SAOUHSC_01778 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.657 |
clpB | dnaJ | SAOUHSC_00912 | SAOUHSC_01682 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | DnaJ protein; 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, DnaK and Gr [...] | 0.979 |
clpB | dnaK | SAOUHSC_00912 | SAOUHSC_01683 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | DNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
clpB | groL | SAOUHSC_00912 | SAOUHSC_02254 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin, 60 kDa, GrpEL, putative; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.795 |
clpB | groS | SAOUHSC_00912 | SAOUHSC_02255 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperonin, 10 kDa, GroES, putative; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.838 |
clpB | grpE | SAOUHSC_00912 | SAOUHSC_01684 | ATP-dependent Clp protease, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB 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 [...] | 0.929 |