| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 [...] | 0.652 |
| atl | clfB | SAOUHSC_00994 | SAOUHSC_02963 | 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 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 [...] | 0.596 |
| atl | ebpS | SAOUHSC_00994 | SAOUHSC_01501 | 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 [...] | 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. | 0.599 |
| atl | fnbA | SAOUHSC_00994 | SAOUHSC_02803 | 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 [...] | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | 0.487 |
| atl | icaA | SAOUHSC_00994 | SAOUHSC_03002 | 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 [...] | Intercellular adhesion protein A, putative; N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Requires IcaD for full activity (By similarity). | 0.711 |
| atl | icaC | SAOUHSC_00994 | SAOUHSC_03005 | 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 [...] | Intercellular adhesion protein C, putative; Presumably involved in the export of the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA) across the cell membrane. | 0.530 |
| atl | icaD | SAOUHSC_00994 | SAOUHSC_03003 | 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 [...] | Conserved hypothetical protein; Necessary for the synthesis of poly-beta-1,6-N-acetyl-D- glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Is required for full IcaA N- acetylglucosaminyltransferase activity (By similarity). | 0.505 |
| atl | icaR | SAOUHSC_00994 | SAOUHSC_03001 | 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 [...] | Ica operon transcriptional regulator IcaR, putative; Represses transcription of the icaADBC operon necessary for biofilm production. | 0.608 |
| 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 [...] | 0.652 |
| 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 | ebpS | SAOUHSC_00812 | SAOUHSC_01501 | 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 [...] | 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. | 0.889 |
| clfA | eno | SAOUHSC_00812 | SAOUHSC_00799 | 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 [...] | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. | 0.751 |
| clfA | fnbA | SAOUHSC_00812 | SAOUHSC_02803 | 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 [...] | Fibronectin-binding protein precursor, putative; Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding sit [...] | 0.901 |
| clfA | icaA | SAOUHSC_00812 | SAOUHSC_03002 | 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 [...] | Intercellular adhesion protein A, putative; N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Requires IcaD for full activity (By similarity). | 0.613 |
| clfA | icaB | SAOUHSC_00812 | SAOUHSC_03004 | 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 [...] | icaB protein, putative; Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D- glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. N-deacetylation is crucial for attachment of the polysaccharide to the bacterial cell surface; it leads to the introduction of positive charges in the otherwise neutral PIA polymer, allowing electrostatic interactions (By similarity). | 0.509 |
| clfA | icaC | SAOUHSC_00812 | SAOUHSC_03005 | 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 [...] | Intercellular adhesion protein C, putative; Presumably involved in the export of the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA) across the cell membrane. | 0.608 |
| clfA | icaD | SAOUHSC_00812 | SAOUHSC_03003 | 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; Necessary for the synthesis of poly-beta-1,6-N-acetyl-D- glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. Is required for full IcaA N- acetylglucosaminyltransferase activity (By similarity). | 0.566 |
| clfA | icaR | SAOUHSC_00812 | SAOUHSC_03001 | 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 [...] | Ica operon transcriptional regulator IcaR, putative; Represses transcription of the icaADBC operon necessary for biofilm production. | 0.418 |
| clfB | atl | SAOUHSC_02963 | SAOUHSC_00994 | 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 [...] | 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 [...] | 0.596 |
| 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 |