| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD29286.1 | sspA | SAOUHSC_00105 | SAOUHSC_00988 | Phosphonate ABC transporter, substrate-binding protein, putative. | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.584 |
| ABD30228.1 | clfA | SAOUHSC_01114 | SAOUHSC_00812 | Fibrinogen-binding protein. | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.618 |
| 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. | 0.522 |
| ABD30228.1 | sspA | SAOUHSC_01114 | SAOUHSC_00988 | Fibrinogen-binding protein. | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.677 |
| atl | clfA | SAOUHSC_00994 | SAOUHSC_00812 | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.647 |
| atl | hly | SAOUHSC_00994 | SAOUHSC_01121 | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | 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. | 0.425 |
| atl | lip2 | SAOUHSC_00994 | SAOUHSC_00300 | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | Lipase precursor. | 0.626 |
| atl | sspA | SAOUHSC_00994 | SAOUHSC_00988 | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.544 |
| atl | sspB | SAOUHSC_00994 | SAOUHSC_00987 | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.446 |
| clfA | ABD30228.1 | SAOUHSC_00812 | SAOUHSC_01114 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Fibrinogen-binding protein. | 0.618 |
| clfA | atl | SAOUHSC_00812 | SAOUHSC_00994 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | 0.647 |
| clfA | hly | SAOUHSC_00812 | SAOUHSC_01121 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 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. | 0.618 |
| clfA | lip2 | SAOUHSC_00812 | SAOUHSC_00300 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Lipase precursor. | 0.489 |
| clfA | sspA | SAOUHSC_00812 | SAOUHSC_00988 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Glutamyl endopeptidase precursor, putative; Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobu [...] | 0.556 |
| clfA | sspB | SAOUHSC_00812 | SAOUHSC_00987 | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | Cysteine protease precursor, putative; Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin- 3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. | 0.447 |
| hly | ABD30228.1 | SAOUHSC_01121 | SAOUHSC_01114 | 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. | Fibrinogen-binding protein. | 0.522 |
| hly | atl | SAOUHSC_01121 | SAOUHSC_00994 | 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. | Bifunctional autolysin precursor, putative; Endohydrolysis of the di-N-acetylchitobiosyl unit in high- mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity); In the C-terminal section; belongs to the glycosyl hydrolas [...] | 0.425 |
| hly | clfA | SAOUHSC_01121 | SAOUHSC_00812 | 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. | Clumping factor; Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen c [...] | 0.618 |
| hly | lip2 | SAOUHSC_01121 | SAOUHSC_00300 | 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. | Lipase precursor. | 0.475 |
| hly | scpA | SAOUHSC_01121 | SAOUHSC_01589 | 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. | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves. | 0.405 |
