node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clfA | clfB | SAOUHSC_00812 | SAOUHSC_02963 | 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 [...] | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.733 |
clfA | sasG | SAOUHSC_00812 | SAOUHSC_02798 | 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 [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.777 |
clfA | srtA | SAOUHSC_00812 | SAOUHSC_02834 | 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 [...] | 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 [...] | 0.643 |
clfB | clfA | SAOUHSC_02963 | SAOUHSC_00812 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 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 [...] | 0.733 |
clfB | sasG | SAOUHSC_02963 | SAOUHSC_02798 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.424 |
clfB | srtA | SAOUHSC_02963 | SAOUHSC_02834 | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 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 [...] | 0.742 |
sasG | clfA | SAOUHSC_02798 | SAOUHSC_00812 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 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 [...] | 0.777 |
sasG | clfB | SAOUHSC_02798 | SAOUHSC_02963 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.424 |
sasG | sdrC | SAOUHSC_02798 | SAOUHSC_00544 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | sdrC protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion. | 0.450 |
sasG | sdrD | SAOUHSC_02798 | SAOUHSC_00545 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | sdrD protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host DSG1 to promote bacterial adhesion to host cells. Contributes to the resistance to killing by innate immune components such as neutrophils present in blood and thus attenuates bacterial clearance. | 0.568 |
sasG | srtA | SAOUHSC_02798 | SAOUHSC_02834 | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 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 [...] | 0.530 |
sdrC | sasG | SAOUHSC_00544 | SAOUHSC_02798 | sdrC protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion. | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.450 |
sdrC | sdrD | SAOUHSC_00544 | SAOUHSC_00545 | sdrC protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion. | sdrD protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host DSG1 to promote bacterial adhesion to host cells. Contributes to the resistance to killing by innate immune components such as neutrophils present in blood and thus attenuates bacterial clearance. | 0.476 |
sdrC | srtA | SAOUHSC_00544 | SAOUHSC_02834 | sdrC protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion. | 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 [...] | 0.443 |
sdrD | sasG | SAOUHSC_00545 | SAOUHSC_02798 | sdrD protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host DSG1 to promote bacterial adhesion to host cells. Contributes to the resistance to killing by innate immune components such as neutrophils present in blood and thus attenuates bacterial clearance. | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.568 |
sdrD | sdrC | SAOUHSC_00545 | SAOUHSC_00544 | sdrD protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host DSG1 to promote bacterial adhesion to host cells. Contributes to the resistance to killing by innate immune components such as neutrophils present in blood and thus attenuates bacterial clearance. | sdrC protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host NRXN1 to promote bacterial adhesion. | 0.476 |
sdrD | srtA | SAOUHSC_00545 | SAOUHSC_02834 | sdrD protein, putative; Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host DSG1 to promote bacterial adhesion to host cells. Contributes to the resistance to killing by innate immune components such as neutrophils present in blood and thus attenuates bacterial clearance. | 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 [...] | 0.700 |
srtA | clfA | SAOUHSC_02834 | SAOUHSC_00812 | 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 [...] | 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 [...] | 0.643 |
srtA | clfB | SAOUHSC_02834 | SAOUHSC_02963 | 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 [...] | Clumping factor B, putative; Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps. Partly responsible for mediating bacterial attachment to the highly keratinized squamous epithelial cells from the nasal cavity via an interaction with cytokeratin K10 (K10). Also promotes bacterial attachment to cultured keratinocytes, possibly through an interaction with cytokeratin K10. Binds mouse cytokeratin K10. Activates human platelet aggregation; Belongs to the s [...] | 0.742 |
srtA | sasG | SAOUHSC_02834 | SAOUHSC_02798 | 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 [...] | Conserved hypothetical protein; Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non- differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation. | 0.530 |