3.4.22.B63: sortase C
This is an abbreviated version!
For detailed information about sortase C, go to the full flat file.
Word Map on EC 3.4.22.B63
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3.4.22.B63
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streptococcus
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pilins
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adhesin
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fimbriae
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actinomyces
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pyogenes
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shaft
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rrgc
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lpxtg
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transpeptidases
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agalactiae
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piliated
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coaggregation
- 3.4.22.B63
- streptococcus
- pilins
- adhesin
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fimbriae
- actinomyces
- pyogenes
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shaft
- rrgc
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lpxtg
- transpeptidases
- agalactiae
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piliated
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coaggregation
Reaction
The enzyme from Bacillus anthracis cleaves the LPNT-/-A sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli [17074072]. The enzymes from Streptococcus pneumoniae and Enterococcus faecalis are required for efficient pilus assembly. =
Synonyms
pilus-associated sortase C, sortase C, sortase C1, sortase C2, sortaseC1, Srt-2, SrtC, SrtC-1, SrtC-2, SrtC-3, SrtC1, SrtC2, SrtC_1, SrtC_2, yhhA
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 3.4.22.B63 - sortase C
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REACTION DIAGRAM
BasH polypeptide + H2O
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sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine. Sortase C substrate BasH is expressed in the forespore
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surface protein containing a QVPTGV motif + H2O
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SrtC2 anchors a surface protein containing a QVPTGV motif (followed by a hydrophobic region and a charged tail) to the cell wall
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sortase C cleaves the LPNTA sorting signal of BasH and BasI, thereby anchoring both polypeptides to the cell wall envelope of sporulating bacilli. Sortase C specifically recognizes and cleaves the LPNTA motif. SrtCDELTAN (with a replacement of the N-terminal signal peptide of sortase C for six histidy) cleaves peptides encompassing the LPNTA motif between threonine and alanine
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BasI polypeptide + H2O
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the LPNTA motif of BasI is cleaved between the threonine and the alanine residue. The C-terminal carboxyl group of threonine is subsequently amide linked to the side chain amino group of diaminopimelic acid within the wall peptides of Bacillus anthracis peptidoglycan (predivisional cell envelope). Sortase C with an active-site cysteine and the LPNTA sorting signal of BasI are required for anchoring of the polypeptide to the cell wall envelope
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preferred substrate of SrtC2
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Dabcyl-ancillary protein 1-Edans + H2O
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Streptococcus agalactiae serogroup V ATCC BAA-611
preferred substrate of SrtC2
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preferred substrate of SrtC1
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Dabcyl-ancillary protein 2-Edans + H2O
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Streptococcus agalactiae serogroup V ATCC BAA-611
preferred substrate of SrtC1
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Dabcyl-BP-1 peptide-Edans + H2O
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Streptococcus agalactiae serogroup V ATCC BAA-611
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assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF
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additional information
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the enzyme is required for efficient pilusassembly
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additional information
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assembly of pili and their cell wall attachment occur via a mechanism of cross-linking of the Ebp proteins (EbpA, EbpB, and EbpC) by SrtC. SrtC is important for biofilm production of Enterococcus faecalis strain OG1RF
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additional information
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of the three genes for structural subunits, rrgB encodes the major pilin, while rrgA and rrgC encode ancillary pilin subunits decorating the pilus shaft and tip. Deletion of all three pilus associated sortase genes, srtB, srtC and srtD, completely prevents pilus biogenesis. Both SrtB and SrtC act as pilus subunit polymerases, with SrtB processing all three pilus subunit proteins, while SrtC processes only RrgB and RrgA
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additional information
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pilus-associated sortase C from Streptococcus pneumoniae acts as a polymerase for the pilus subunit proteins RrgA and RrgB
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additional information
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SrtC-1, SrtC-2, and SrtC-3 are responsible for RlrA pilus assembly and exhibit functional redundancy with respect to backbone assembly and cell wall localization. SrtC-3 is required for the incorporation of the accessory subunits RrgA and RrgC. Deleterious effect on pilus assembly upon alteration of the cell wall sorting signals of the accessory subunit proteins
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