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
-
sortase-mediated
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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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Substrates Products
Substrates Products on EC 3.4.22.70 - sortase A
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REACTION DIAGRAM
2-aminobenzoyl-LPATG-diaminopropionic acid + H2O
2-aminobenzoyl-LPAT + G-diaminopropionic acid
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efficient cleavage
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-
?
2-aminobenzoyl-LPNTA-diaminopropionic acid + H2O
2-aminobenzoyl-LPNT + A-diaminopropionic acid
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small amount of cleavage
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-
?
4-([4-(dimethylamino)phenyl]-azo)-benzoyl-QALPETGEE-((2-aminoethyl)-amino)naphthalene-1-sulfonic acid + H2O
?
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a catalytically important and conserved binding surface is formed by residues A118, T180 and I182. R197 is also required for catalysis
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-
?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Gln-Ala-Leu-Pro-Glu-Thr-Gly-Glu-Glu-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Gln-Ala-Leu-Pro-Glu-Thr + Gly-Glu-Glu-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
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-
-
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?
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Leu-Pro-Glu-Thr-Gly-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoyl-Leu-Pro-Glu-Thr + Gly-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
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-
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?
5(6)-carboxyfluorescein-6-aminohexanoic acid-LPKTGGRR-NH2 + H2O
?
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?
A33-LPETG-His6 + H2O
?
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A33 antigen extracellular domain bearing a His6 tag
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-
?
Abz-KVENPQTNAGT-Dap(Dnp)-NH2 + GGGGG
Abz-KVENPQTGGGGG + Gly-Dap(DNP)-NH2
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?
Abz-LPETG-Dap(Dnp)-NH2 + GGGGG
Abz-LPETGGGGGG + Gly-Dap(Dnp)-NH2
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?
Abz-LPETG-Dap(Dnp)-NH2 + Gly5
?
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transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic NH2-Ala2
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-
?
Abz-LPETG-Dap(Dnp)-NH2 + Gly5
Abz-LPETGGGGG-OH + Gly-Dap(Dnp)-NH2
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?
Abz-LPETGG-Dap(Dnp)-NH2 + GGGGG
Abz-LPETGGGGGG + Gly-Dap(Dnp)-NH2
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?
Abz-LPKTGK(Dnp)KK + GGGWW
Abz-LPKTGGGWW + GK(Dnp)KK
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substrate peptide 1 (Abz-LPKTGK(Dnp)KK) and acceptor peptide 2 (GGGWW)
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-
?
acetyl-ooocctcttacctcagttacaoooLPKTGGR-NH2 + H-GGGKLALKLALKALKAALKLA-NH2
acetyl-ooocctcttacctcagttacaoooLPKTGGGKLALKLALKALKAALKLA-NH2 + H-GGR-NH2
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-
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?
agmatine + YALPETGK
(NH2)2-CN-(CH2)4-NH-(CO)-TEPLAY + ?
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transpeptidase reaction. The initially formed acyl-enzyme intermediate undergoes a hydrolysis followed by intra-molecular transpeptidation
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?
AHLPKTGLR + 6-aminohexyl 4-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
?
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?
aminobenzoyl-LPETG-dinitrophenyl ester + Gly-Gly-Gly
aminobenzoyl-LPETGGG + Gly-dinitrophenyl ester
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HPLC results provide direct evidence for the formation of the kinetically competent acyl enzyme intermediate
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?
Dns-LPKTGGRR + GGGWW
Dns-LPKTGGGWW + GGRR
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dansyl-labeled Dns-LPKTGGRR substrate peptide and acceptor peptide 2 (GGGWW)
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-
?
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester + Gly-Gly-Gly
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-Gly-Gly + Gly-2,4-dinitrophenyl ester
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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. The S1' and S2' sites of the sortase both prefer a glycine residue, the S1' site is exclusively selective for glycine
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?
o-aminobenzoyl-Leu-Pro-Glu-Thr-Gly-2,4-dinitrophenyl ester + H2O
o-aminobenzoyl-Leu-Pro-Glu-Thr + Gly-2,4-dinitrophenyl ester
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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. The S1' and S2' sites of the sortase both prefer a glycine residue, the S1' site is exclusively selective for glycine
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?
o-aminobenzoyl-LPETG-2,4-dinitrophenyl + H2O
o-aminobenzoyl-LPETG + 2,4-dinitrophenol
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?
recombinant Helicobacter pylori R1,3-fucosyltransferase + triglycine
?
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?
recombinant human beta1,4-galactosyltransferase + N-(2-(2-ethoxyethoxy)ethanamine)biotin amide
?
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?
recombinant human beta1,4-galactosyltransferase + N-hexylbiotin amide
?
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?
[4-(4-dimethylaminophenylazo)benzoic acid]-QALPETGEE-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
?
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?
Abz-LPETG-Dap(Dnp) + H2O
?
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evidence for a reverse protonation catalytic mechanism
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-
?
Abz-LPET + G-Dap(Dnp)
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cleavage between the threonine and the glycine residues, efficient cleavage
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-
?
Abz-LPETAA + GG-Dap(Dnp)-NH2
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic AlaAla
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?
Abz-LPETGG-Dap(Dnp)-NH2 + Ala-Ala
Abz-LPETAA + GG-Dap(Dnp)-NH2
transpeptidation of LPXTG-containing peptides to the cell-wall precursor mimic AlaAla
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?
Dabcyl-QALPET + GEE-Edans
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?
Dabcyl-QALPETGEE-Edans + H2O
Dabcyl-QALPET + GEE-Edans
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?
?
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the substrate mimicks the LPXTG motif of pilus 2a minor ancillary protein
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?
Dabcyl-SFLPKTGM-EDANS + H2O
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the substrate mimicks the LPXTG motif of pilus 2a minor ancillary protein
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?
?
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G-eGFP = enhanced green fluorescent protein with a glycine at the N-terminus, protein-protein ligation reaction
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?
GST-LPETG + G-eGFP
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G-eGFP = enhanced green fluorescent protein with a glycine at the N-terminus, protein-protein ligation reaction
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?
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sortase A may be critical in the early stage of inhaltation anthrax
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additional information
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no cleavage of 2-aminobenzoyl-NPKTG-diaminopropionic acid and 2-aminobenzoyl-LGATG-diaminopropionic acid
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additional information
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SrtA recognizes the LPXTG-sorting signal through a lock-in-key mechanism
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additional information
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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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additional information
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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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additional information
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sortase localization is facilitated by a positive charge that is necessary for efficient pilus biogenesis
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additional information
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non-gel proteomics is a powerful technique to rapidly identify sortase substrates and to gain insights on potential sorting motifs. LPXTG-containing proteins were identified exclusively in strains having a functional SrtA
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additional information
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the enzyme anchors surface proteins to the bacterial cell wall
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additional information
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the enzyme anchors surface proteins to the bacterial cell wall
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additional information
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the enzyme cleaves surface proteins of Staphylococcus aureus at the LPXT-/-G motif
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additional information
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the enzyme cleaves surface proteins of Staphylococcus aureus at the LPXT-/-G motif
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additional information
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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 LPET-/-G 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. The S1' and S2' sites of the sortase both prefer a glycine residue, the S1' site is exclusively selective for glycine
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additional information
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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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additional information
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the enzyme anchors surface proteins to the bacterial cells wall
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additional information
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the enzyme anchors surface proteins to the bacterial cells wall
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additional information
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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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additional information
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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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additional information
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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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additional information
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primary role of the SrtA isoform in Staphylococcus aureus adhesion and host colonization
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additional information
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the transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
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additional information
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sortase A plays a role in the establishment of infections
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additional information
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sortase can transfer peptide substrates to oligosaccharides appended with a 6-deoxy-6-aminohexose moiety in a selective manner as that of an oligoglycine sequence
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additional information
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SrtA cleaves proteins at LPXTG-motif between threonine and glycine, and subsequently transfers the acyl-fragment to a N-terminal oligoglycine
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additional information
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SrtA recognizes LPXTG near the C-terminus of a target protein. The Cys184 of SrtA performs a nucleophilic attack at the peptide bond between T and G in LPXTG, resulting in a thioester intermediate with the carboxyl group of the C-terminal T linked to Cys184. This reactive intermediate reacts with the cross-bridge N-terminus of a cell-wall proteoglycan to anchor the target protein to the cell-wall peptidoglycan. SrtA accepts various peptide/protein substrates, so long as they bear the sorting signal LPXTG, and a range of amino nucleophiles
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additional information
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the enzyme cleaves the LPXTG sequence at the amide bond between the threonine and the glycine to form an acyl-enzyme complex. Nucleophilic attack by the amino group of the tri-glycine on the intermediate results in the formation of an LPXT-GGG bond and the liberation of the free enzyme
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additional information
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no activity with Dabcyl-KGIIPKTGGK-Edans, Dabcyl-KKVTIPQTGGIGT-Edans and Dabcyl-SFIPKTGM-Edans
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additional information
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sortase A also mediates transpeptidation reaction of indolicidin-derived peptides
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additional information
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sortase A mediates either head to tail cyclization or oligomerization and then head to tail cyclization of peptides (e.g. GGVTSAPDTLPKTGGS) and glycopeptides (e.g. MUC1 glycopeptide), depending on the peptide length, to produce 15-mer or higher cyclic peptides and glycopeptides
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additional information
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sortase A optimal cleavage site is LPETGG
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additional information
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sortase-mediated cyclization of histatin-1 (GG-histatin 1-LPETGG) provides a yield of more than 90%
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additional information
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truncated SrtADELTAN40 also catalyzes in vitro transpeptidation reaction
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additional information
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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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additional information
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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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additional information
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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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additional information
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semienzymatic cyclization of disulfide-rich peptides using sortase A, including the cyclotide kalata B1, alpha-conotoxin Vc1.1, and sunflower trypsin inhibitor 1, without the need for a thioester linker and using Fmoc chemistry, NMR spectral structure analysis, overview
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additional information
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the enzyme is highly selective and does not require any cofactors for the catalysis of protein ligation, but it is unable to access the recognition site within the highly structured regions of folded substrates. Ligation of purified glutathione-S-transferase and green fluorescence protein by recombinant circular enzyme
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?
additional information
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no activity with Dabcyl-KGIIPKTGGK-Edans, Dabcyl-KKVTIPQTGGIGT-Edans and Dabcyl-SFIPKTGM-Edans
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?
additional information
?
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truncated SrtADELTAN40 also catalyzes in vitro transpeptidation reaction
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?
additional information
?
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the enzyme is highly selective and does not require any cofactors for the catalysis of protein ligation, but it is unable to access the recognition site within the highly structured regions of folded substrates. Ligation of purified glutathione-S-transferase and green fluorescence protein by recombinant circular enzyme
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?
additional information
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sortase A plays a role in the establishment of infections
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additional information
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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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additional information
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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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additional information
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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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additional information
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SrtA is dispensable for pilus assembly and localization to the cell wall
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additional information
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SrtA contributes to antiopsonization in Streptococci. SrtA anchors surface adhesins as well as some proteins that function as antiopsonic molecules as a means of evading the human immune system. SrtA of Streptococcus sanguinis plays important roles in bacterial colonization
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additional information
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SrtA is involved in the virulence manifestation of streptococcal toxic shock syndrome
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additional information
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sortase A anchors the following proteins in the cell wall of Streptococcus uberis strain 0140J: putative fructan beta-fructosidase precursor, putative lactoferrin binding protein, putative collagen-like surface anchored protein, putative C5a peptidase precursor, and putative zinc-carboxypeptidase. Alternate cell wall anchoring motifs are either LPXTXD/E or LPXXXD
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?