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
-
lpxtg
- streptococcus
- peptidoglycan
-
transpeptidation
-
sortase-mediated
-
a-mediated
- adhesins
-
bioconjugation
-
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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General Information
General Information on EC 3.4.22.70 - sortase A
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malfunction
physiological function
additional information
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deletion of srtA affects the attachment stage and results in a deficiency in biofilm production, deletion of srtA has no effect on cell viability and cell growth
malfunction
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deficiency of srtA impairs the release of pro-inflammatory cytokines in Staphylococcus aureus-induced mastitis. A DEKTASrtA mutant strain attenuates the inflammatory reaction in the mammary tissue of mice compared with wild-type Staphylococcus aureus challenge. The enzyme mutant strain impairs the induction of pro-inflammatory cytokines such as tumor necrosis factor-alpha, interleukin-1beta, and interleukin-6, the mutant strain blocks the activation of nuclear factor kappaB and mitogen-activated protein kinases by attenuating the degradation and phosphorylation of signaling pathway molecules such as IkappaBalpha, p65 and p38.
malfunction
the deletion of sortase A affects the virulence and infectious capacity of Streptococcus iniae
malfunction
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the deletion of sortase A affects the virulence and infectious capacity of Streptococcus iniae
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malfunction
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deficiency of srtA impairs the release of pro-inflammatory cytokines in Staphylococcus aureus-induced mastitis. A DEKTASrtA mutant strain attenuates the inflammatory reaction in the mammary tissue of mice compared with wild-type Staphylococcus aureus challenge. The enzyme mutant strain impairs the induction of pro-inflammatory cytokines such as tumor necrosis factor-alpha, interleukin-1beta, and interleukin-6, the mutant strain blocks the activation of nuclear factor kappaB and mitogen-activated protein kinases by attenuating the degradation and phosphorylation of signaling pathway molecules such as IkappaBalpha, p65 and p38.
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Bacillus anthracis uses the sortase A enzyme to anchor proteins to its cell wall envelope during vegetative growth
physiological function
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intraperitoneal immunization with recombinant SrtA confers to mice protection against Streptococcus pneumoniae intraperitoneal challenge
physiological function
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intraperitoneal immunization with recombinant SrtA confers to mice protection against Streptococcus pneumoniae intraperitoneal challenge
physiological function
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intraperitoneal immunization with recombinant SrtA confers to mice protection against Streptococcus pneumoniae intraperitoneal challenge
physiological function
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sortase A catalyzes cell wall anchoring reaction of LPXTG surface proteins
physiological function
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sortase A covalently attaches proteins to the bacterial cell wall by cleaving between threonine and glycine at an LPXTG recognition motif
physiological function
sortase A is involved in cell wall anchoring of pilus polymers
physiological function
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the enzyme catalyzes the covalent anchoring of surface proteins to the cell wall by linking the threonyl carboxylate of the LPXTG recognition motif to the amino group of the pentaglycine cross-bridge of the peptidoglycan
physiological function
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the enzyme is responsible for the cell wall anchoring of LPXTG-containing proteins
physiological function
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as a transpeptidase that covalently attaches various virulence factors to the cell surface, this enzyme plays a crucial role in the ability of bacteria to invade the host's tissues and to escape the immune response
physiological function
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sortase A is a key virulence factor in the pathogenesis of Staphylococcus aureus-induced mastitis in mice, overview
physiological function
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the enzyme is responsible for the cell wall anchoring of LPXTG-containing proteins
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physiological function
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sortase A is involved in cell wall anchoring of pilus polymers
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physiological function
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sortase A is a key virulence factor in the pathogenesis of Staphylococcus aureus-induced mastitis in mice, overview
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binding mechanism is a conformational selection followed by induced fit, and allosteric regulation of the enzyme, molecular dynamics simulations of the enzyme in apo state and when bound to an LPATG sorting signal, which adopts multiple metastable states, overview. The first and the second substrate binding sites are proposed to be located on opposing faces of the protein. The active sites of all sortases contain a conserved catalytic triad that consists of residues H120, C184, and R197. NMR SrtA structure covalently bound to a modified sorting signal, binding conformations, overview
additional information
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binding mechanism is a conformational selection followed by induced fit, and allosteric regulation of the enzyme, molecular dynamics simulations of the enzyme in apo state and when bound to an LPATG sorting signal, which adopts multiple metastable states, overview. The first and the second substrate binding sites are proposed to be located on opposing faces of the protein. The active sites of all sortases contain a conserved catalytic triad that consists of residues H120, C184, and R197. NMR SrtA structure covalently bound to a modified sorting signal, binding conformations, overview
additional information
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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, mechanism, overview
additional information
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sortase A mediates site-specific immobilization for identification of protein interactions in affinity purification-mass spectrometry experiments, overview
additional information
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substrate-induced conformational dynamics in the enzyme, roles of invariant Leu and Pro residues of the substrate in modulating the enzyme dynamics, analysis of the selection process of a catalytically competent substrate, molecular dynamics simulations with noncanonical substrates, overview. The linked conformation due to Pro in LPXTG is obligatory for productive binding but does not per se control the enzyme dynamics. The Leu residue of the substrate appears to play the crucial role of an anchor to the beta6-beta7 loop directing the conformational transition of the enzyme from an open to a closed state subsequent to which the Pro residue facilitates the consummation of binding through predominant engagement of the loop and catalytic motif residues in hydrophobic interactions, molecular dynamics simulations, overview
additional information
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the structural integrity of circular sortase A and its biochemical characteristics are compared to those of the linear enzyme analog and are similar under native conditions, overview. Circular enzyme is active at concentrations of urea up to 3 M and is capable of efficient catalytic protein-protein coupling, while the linear enzyme is unable to mediate the ligation of substrate proteins under the same conditions
additional information
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the structural integrity of circular sortase A and its biochemical characteristics are compared to those of the linear enzyme analog and are similar under native conditions, overview. Circular enzyme is active at concentrations of urea up to 3 M and is capable of efficient catalytic protein-protein coupling, while the linear enzyme is unable to mediate the ligation of substrate proteins under the same conditions
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