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SpeB
(Streptococcal pyrogenic exotoxin B) |
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Integrin-binding cysteine protease secreted in a zymogen form (40-kDa, 371 residues) and autocatalytically cleaved N terminal 118 residues to generate the mature proteinase. A distant homologue of the papain superfamily that includes that mammalian cathepsins B, K, L and S. Intergrin-binding Arg-Gly-Asp(RGD) motif. PDB code: 1DKI. ... |
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SpeB
(Streptococcal pyrogenic exotoxin B) |
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Integrin-binding cysteine protease secreted in a zymogen form (40-kDa, 371 residues) and autocatalytically cleaved N terminal 118 residues to generate the mature proteinase. A distant homologue of the papain superfamily that includes that mammalian cathepsins B, K, L and S. Intergrin-binding Arg-Gly-Asp(RGD) motif. PDB code: 1DKI. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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Pla
(Plasminogen activator) |
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Belongs to the family of OM proteases/adhesins known as omptins that share high sequence identity but differ in biological function. Omptins appear to constitute a unique class of proteases. Other omptin family outer membrane proteases include PgtE from S. enterica, OmpT and OmpR from E. coli, and SopA/IcsP from S. flexneri. Their catalytic residues are conserved. They require the presence of rough LPS for enzymatic activity and are inhibited by the O-antigen chains present in smooth LPS. Unique to Y. pestis encoded by the pPCP1 plasmid not present in the enteropathogenic yersiniae Y. pseudotuberculosis and Y. enterocolitica. ... |
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