| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hysA | lip2 | SAOUHSC_02463 | SAOUHSC_00300 | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | Lipase precursor. | 0.464 |
| hysA | sspA | SAOUHSC_02463 | SAOUHSC_00988 | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | 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 [...] | 0.482 |
| hysA | sspB | SAOUHSC_02463 | SAOUHSC_00987 | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | 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. | 0.441 |
| hysA | sspC | SAOUHSC_02463 | SAOUHSC_00986 | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.435 |
| lip2 | hysA | SAOUHSC_00300 | SAOUHSC_02463 | Lipase precursor. | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | 0.464 |
| lip2 | sspA | SAOUHSC_00300 | SAOUHSC_00988 | Lipase precursor. | 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 [...] | 0.540 |
| lip2 | sspB | SAOUHSC_00300 | SAOUHSC_00987 | Lipase precursor. | 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. | 0.514 |
| lip2 | sspC | SAOUHSC_00300 | SAOUHSC_00986 | Lipase precursor. | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.450 |
| scpB | sspB | SAOUHSC_01588 | SAOUHSC_00987 | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves. | 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 |
| scpB | sspC | SAOUHSC_01588 | SAOUHSC_00986 | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves. | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.447 |
| sspA | hysA | SAOUHSC_00988 | SAOUHSC_02463 | 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 [...] | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | 0.482 |
| sspA | lip2 | SAOUHSC_00988 | SAOUHSC_00300 | 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 [...] | Lipase precursor. | 0.540 |
| sspA | sspB | SAOUHSC_00988 | SAOUHSC_00987 | 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 [...] | 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. | 0.842 |
| sspA | sspC | SAOUHSC_00988 | SAOUHSC_00986 | 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 [...] | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.752 |
| sspB | hysA | SAOUHSC_00987 | SAOUHSC_02463 | 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. | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | 0.441 |
| sspB | lip2 | SAOUHSC_00987 | SAOUHSC_00300 | 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. | Lipase precursor. | 0.514 |
| sspB | scpB | SAOUHSC_00987 | SAOUHSC_01588 | 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. | Conserved hypothetical protein; Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves. | 0.447 |
| sspB | sspA | SAOUHSC_00987 | SAOUHSC_00988 | 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. | 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 [...] | 0.842 |
| sspB | sspC | SAOUHSC_00987 | SAOUHSC_00986 | 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. | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | 0.984 |
| sspC | hysA | SAOUHSC_00986 | SAOUHSC_02463 | Cysteine protease, putative; Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology; Belongs to the protease inhibitor I57 (SspC) family. | Hyaluronate lyase; Belongs to the polysaccharide lyase 8 family. | 0.435 |
