3.4.22.10: streptopain
This is an abbreviated version!
For detailed information about streptopain, go to the full flat file.
Word Map on EC 3.4.22.10
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3.4.22.10
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speb
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streptococci
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glomerulonephritis
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zymogen
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fasciitis
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superantigens
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streptolysin
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nephritogenic
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streptokinase
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poststreptococcal
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scarlet
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apsgn
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shock-like
- 3.4.22.10
- speb
- streptococci
- glomerulonephritis
- zymogen
- fasciitis
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superantigens
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streptolysin
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nephritogenic
- streptokinase
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poststreptococcal
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scarlet
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apsgn
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shock-like
Reaction
preferential cleavage with hydrophobic residues at P2, P1 and P1' =
Synonyms
EC 3.4.4.18, IdeS, IgG-degrading enzyme of Streptococcus pyogenes, interleukin-1beta convertase, More, proteinase, streptococcal, pyrogenic exotoxin B, SCP, SpcCEP, Spe B, SPE B protease, SPE B/SCP, SpeB, SPP, Steptococcus proteinase, streptococcal cysteine protease, Streptococcal cysteine proteinase, streptococcal erythrogenic toxin B, streptococcal proteinase, streptococcal pyogenic exotoxin B, streptococcal pyrogenic exotoxin B, streptococcal pyrogenic exotoxin B/cysteine protease, Streptococcus peptidase A, Streptococcus protease, streptopain
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General Information on EC 3.4.22.10 - streptopain
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
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wild type strain efficiently translocates across the epithelial monolayer along with cleavage of occludin and E-cadherin. Deletion of the speB gene compromises those activities. Destabilization of the junctional proteins is relieved in cells infected with the speB mutant, as compared with those infected with the wild type
metabolism
physiological function
metabolism
the endopeptidase PepO is a growth phase dependent regulator of SpeB in the invasive GAS M1 serotype strain 5448. PepO influences growth phase-dependent induction of speB gene expression
metabolism
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the endopeptidase PepO is a growth phase dependent regulator of SpeB in the invasive GAS M1 serotype strain 5448. PepO influences growth phase-dependent induction of speB gene expression
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physiological function
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addition of SpeB to human plasma increases plasma-mediated bacterial killing and prolonged coagulation time through the intrinsic pathway of coagulation. This effect is independent of the enzymatic activity of SpeB and is mediated by a noncovalent medium-affinity binding and modification of alpha-1 antitrypsin
physiological function
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in infected mice, SpyCEP expression by Streptococcus pyogenes hinders bacterial clearance from muscle, and enhances bacterial spread, associated with cleavage of CXCL1. SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues. SpyCEP enhances Streptococcus pyogenes dissemination to lower respiratory tract from nasopharynx
physiological function
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the streptococcal regulator of virulence control of SpeB production is a mechanism to regulate biofilm dispersal and provides a mechanism by which mild infection can transition to severe disease
physiological function
streptopain is a critical virulence factor for pathogenesis
physiological function
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addition of SpeB to human plasma increases plasma-mediated bacterial killing and prolonged coagulation time through the intrinsic pathway of coagulation. This effect is independent of the enzymatic activity of SpeB and is mediated by a noncovalent medium-affinity binding and modification of alpha-1 antitrypsin
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physiological function
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the streptococcal regulator of virulence control of SpeB production is a mechanism to regulate biofilm dispersal and provides a mechanism by which mild infection can transition to severe disease
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physiological function
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in infected mice, SpyCEP expression by Streptococcus pyogenes hinders bacterial clearance from muscle, and enhances bacterial spread, associated with cleavage of CXCL1. SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues. SpyCEP enhances Streptococcus pyogenes dissemination to lower respiratory tract from nasopharynx
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physiological function
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the streptococcal regulator of virulence control of SpeB production is a mechanism to regulate biofilm dispersal and provides a mechanism by which mild infection can transition to severe disease
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physiological function
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addition of SpeB to human plasma increases plasma-mediated bacterial killing and prolonged coagulation time through the intrinsic pathway of coagulation. This effect is independent of the enzymatic activity of SpeB and is mediated by a noncovalent medium-affinity binding and modification of alpha-1 antitrypsin
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