3.4.22.71: sortase B
This is an abbreviated version!
For detailed information about sortase B, go to the full flat file.
Word Map on EC 3.4.22.71
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3.4.22.71
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aureus
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peptidoglycan
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anthracis
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envelope
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transpeptidases
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cross-bridges
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isdc
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pentaglycine
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pilin
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transpeptidation
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analysis
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medicine
- 3.4.22.71
- aureus
- peptidoglycan
- anthracis
- envelope
- transpeptidases
-
cross-bridges
- isdc
- pentaglycine
- pilin
-
transpeptidation
- analysis
- medicine
Reaction
The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a NPXTN motif is cleaved. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. =
Synonyms
CD630_27180, class B sortase, CPE0513, sortase B, Spy0129, SrtB, StrB
ECTree
3.4.22.71 sortase BAdvanced search results
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results (General Information
General Information on EC 3.4.22.71 - sortase B
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme is a member of the sortase cysteine transpeptidase family. Members of this enzyme superfamily are widely distributed in Gram-positive bacteria that frequently utilize multiple sortases to elaborate their peptidoglycan, and the family members have a conserved active site His-Cys-Arg triad that joins a sorting signal located at the C-terminus of their protein substrate to an amino nucleophile located on the cell surface
physiological function
additional information
physiological function
sortase attaches hemoproteins to the cell wall
physiological function
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the class B sortase is involved in pilus assembly
physiological function
sortase cysteine transpeptidases covalently attach proteins to the bacterial cell wall or assemble fiber-like pili that promote bacterial adhesion
physiological function
SrtB has dual functions, anchoring AbpA to the cell wall and processing AbpA into a ladder profile. Streptococci adapted to the oral environment rich in salivary amylase display a sortase/adhesion substrate system
physiological function
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the class B sortase is involved in pilus assembly
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physiological function
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SrtB has dual functions, anchoring AbpA to the cell wall and processing AbpA into a ladder profile. Streptococci adapted to the oral environment rich in salivary amylase display a sortase/adhesion substrate system
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additional information
analysis of the substrate binding structure of the enzyme using SrtB-NPQT complexes, by computational modeling, molecular dynamics simulations, and targeted amino acid mutagenesis revealing that the backbone amide of Glu224 and the side chain of Arg233 form an oxyanion hole in sortase B that stabilizes high energy tetrahedral catalytic intermediates. A highly conserved threonine residue within the bound sorting signal substrate facilitates construction of the oxyanion hole by stabilizing the position of the active site arginine residue via hydrogen bonding
additional information
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analysis of the substrate binding structure of the enzyme using SrtB-NPQT complexes, by computational modeling, molecular dynamics simulations, and targeted amino acid mutagenesis revealing that the backbone amide of Glu224 and the side chain of Arg233 form an oxyanion hole in sortase B that stabilizes high energy tetrahedral catalytic intermediates. A highly conserved threonine residue within the bound sorting signal substrate facilitates construction of the oxyanion hole by stabilizing the position of the active site arginine residue via hydrogen bonding
