3.4.21.110: C5a peptidase
This is an abbreviated version!
For detailed information about C5a peptidase, go to the full flat file.
Word Map on EC 3.4.21.110
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3.4.21.110
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streptococci
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pyogenes
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serotype
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agalactiae
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pharyngitis
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medicine
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streptolysin
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streptokinase
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chemotaxins
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antiphagocytic
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dysgalactiae
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m-like
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lancefield
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impetigo
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equisimilis
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pyrogenic
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spycep
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laminin-binding
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fasciitis
- 3.4.21.110
- streptococci
- pyogenes
-
serotype
- agalactiae
- pharyngitis
- medicine
-
streptolysin
- streptokinase
-
chemotaxins
-
antiphagocytic
- dysgalactiae
-
m-like
-
lancefield
- impetigo
- equisimilis
-
pyrogenic
-
spycep
-
laminin-binding
- fasciitis
Reaction
the primary cleavage site is at His67-/-Lys68 in human C5a with a minor secondary cleavage site at Ala58-/-Ser59 =
Synonyms
C5a peptidase, GBS, GBS C5a peptidase, S08.020, SCFI, SCPA, ScpB, scpI, SCPZ, SEZ C5a peptidase, streptococcal chemotactic factor inactivator, surface-bound C5a peptidase
ECTree
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Engineering
Engineering on EC 3.4.21.110 - C5a peptidase
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D130A
H193A
N295A
S512A
D130A
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strain 90 226 SCPA-mutant, impaired capacity to infect nasal mucosa-associated lymphoid tissue
additional information
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analysis of M-like protein (simA) and C5a peptidase, two gene homologues of Streptococcus iniae, through allelic replacement reveals that M-like protein plays a significant role in Streptococcus iniae virulence and C5a peptidase does not
additional information
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isogenic M1-mutant, expressses SCPA on cell surface
additional information
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mutant ScpBdelta, a common natural variant of ScpB, contains a 4-amino-acid deletion that eliminates peptidase activity. High affinity for fibronectin is maintained in ScpBdelta. ScpB and scpBdelta can complement the fibronectin-binding defect of the deletion mutant strain TOH97, that does not express scpB. Thus, the delta12 allele has no effect on the fibronectin binding of recombinant ScpB, recombinant ScpB-phage display fragment, or ScpB expressed by group B streptococci. High-affinity interaction between ScpB and immobilized fibronectin is responsible for the maintenance of the scpB gene in strains lacking C5a peptidase activity
additional information
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mutant ScpBdelta, a common natural variant of ScpB, contains a 4-amino-acid deletion that eliminates peptidase activity. High affinity for fibronectin is maintained in ScpBdelta. ScpB and scpBdelta can complement the fibronectin-binding defect of the deletion mutant strain TOH97, that does not express scpB. Thus, the delta12 allele has no effect on the fibronectin binding of recombinant ScpB, recombinant ScpB-phage display fragment, or ScpB expressed by group B streptococci. High-affinity interaction between ScpB and immobilized fibronectin is responsible for the maintenance of the scpB gene in strains lacking C5a peptidase activity
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