3.4.22.70: sortase A
This is an abbreviated version!
For detailed information about sortase A, go to the full flat file.
Word Map on EC 3.4.22.70
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3.4.22.70
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aureus
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staphylococcus
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lpxtg
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streptococcus
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peptidoglycan
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transpeptidation
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sortase-mediated
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a-mediated
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adhesins
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bioconjugation
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antivirulence
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mutans
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anti-infective
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pilins
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transpeptidases
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oligoglycine
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cross-bridges
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pentaglycine
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wall-anchored
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molecular biology
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azide-alkyne
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analysis
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biotechnology
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drug development
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synthesis
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medicine
- 3.4.22.70
- aureus
- staphylococcus
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lpxtg
- streptococcus
- peptidoglycan
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transpeptidation
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sortase-mediated
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a-mediated
- adhesins
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bioconjugation
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antivirulence
- mutans
-
anti-infective
- pilins
- transpeptidases
-
oligoglycine
-
cross-bridges
- pentaglycine
-
wall-anchored
- molecular biology
-
azide-alkyne
- analysis
- biotechnology
- drug development
- synthesis
- medicine
Reaction
The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. =
Synonyms
C60.001, sortase A, sortase A transpeptidase, sortase SrtA, sortase transpeptidase, SrtA, SrtA protein, SrtA sortase
ECTree
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Natural Substrates Products on EC 3.4.22.70 - sortase A
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REACTION DIAGRAM
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two elements of Spa pilin precursor, the pilin motif and the sorting signal, are together sufficient to promote the polymerization of an otherwise secreted protein by a process requiring the function of the sortase A
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two elements of Spa pilin precursor, the pilin motif and the sorting signal, are together sufficient to promote the polymerization of an otherwise secreted protein by a process requiring the function of the sortase A
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sortase localization is facilitated by a positive charge that is necessary for efficient pilus biogenesis
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transpeptidase activity: the enzyme catalyzes a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXT-/-G motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. When a nucleophile is not available, sortase slowly hydrolyzes the LPETG peptide at the same site. Ping-pong mechanism in which a common acyl-enzyme intermediate is formed in transpeptidation and hydrolysis. The nucleophile binding site of the enzyme is specific for diglycine
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the enzyme anchors surface proteins to the bacterial cells wall
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the enzyme anchors surface proteins to the bacterial cells wall
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the enzyme cleaves surface proteins of Staphylococcus aureus at the LPXT-/-G motif, catalyzes surface protein anchoring by means of a transpeptidation reaction that captures cleaved polypeptides as thioester enzyme intermediates
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the enzyme cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of Thr and the amino group of cell-wall crossbridges
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gram-positive pathogenic bacteria display proteins on their surface that play important roles during infection. In Staphylococcus aureus theses surface proteins are anchored to the cell wall by two sortase, sortase A and sortaseB that recognize specific surface protein sorting signals. Sortase A is an essential virulence factor for establishment of septic arthritis
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primary role of the SrtA isoform in Staphylococcus aureus adhesion and host colonization
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the transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
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Surface proteins destined for cell wall anchoring contain a LPXTG sequence located in their C-terminus which serves as a substrate recognition motif for SrtA
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the bacterial transpeptidase sortase A catalyzes the chemoselective ligation of peptides and proteins. During catalysis sortase A cleaves the conserved Leu-Pro-X-Thr-Gly sorting motif at the Thr residue under concomitant thioester formation at active site Cys184
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the enzyme recognizes a 5-residue sequence motif, LPXTG, and cleaves the peptide bond between the Thr and Gly residues, forming an acyl enzyme intermediate between a cysteine at the active site of SrtA and the carboxylate at the truncated C-terminus of the substrate
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SrtA sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine
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in addition to its role in processing LPXTG containing adhesins, sortase A has the function of contributing to transcriptional regulation of adhesin gene expression
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role of srtA in adherence in vitro is dependent on capsule expression, the role of SrtA in adherence to human cells only being apparent in the absence of the pneumococcal capsule
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SrtA is dispensable for pilus assembly and localization to the cell wall
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SrtA is involved in the virulence manifestation of streptococcal toxic shock syndrome
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