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Literature summary extracted from

  • Budzik, J.M.
    Oh, S.Y.; Schneewind, O.: Cell wall anchor structure of BcpA pili in Bacillus anthracis (2008), J. Biol. Chem., 283, 36676-3686.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.B64 C207A although sortase C207A is expressed at the same level as the wild-type enzyme, the mutant was unable to cleave IsdX1SS-GST substrate Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.B64 pilin protein BcpA + H2O Bacillus anthracis the major pilin protein BcpA is cleaved between the threonine and the glycine of its C-terminal LPXTG motif sorting signal. The resulting acyl enzyme intermediate is relieved by the nucleophilic attack of the side-chain amino group of lysine within the YPKN motif of another BcpA subunit. Cell wall anchoring of assembled BcpA pili requires sortase A, which also cleaves the LPXTG sorting signal of BcpA between its threonine and glycine residues ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.B64 Bacillus anthracis
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.B64 pilin protein BcpA + H2O the major pilin protein BcpA is cleaved between the threonine and the glycine of its C-terminal LPXTG motif sorting signal. The resulting acyl enzyme intermediate is relieved by the nucleophilic attack of the side-chain amino group of lysine within the YPKN motif of another BcpA subunit. Cell wall anchoring of assembled BcpA pili requires sortase A, which also cleaves the LPXTG sorting signal of BcpA between its threonine and glycine residues Bacillus anthracis ?
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 ?
3.4.22.B64 pilin protein BcpA + H2O the major pilin protein BcpA is cleaved between the threonine and the glycine of its C-terminal LPXTG motif sorting signal. The resulting acyl enzyme intermediate is relieved by the nucleophilic attack of the side-chain amino group of lysine within the YPKN motif of another BcpA subunit Bacillus anthracis ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.B64 pilin-specific sortase D
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 Bacillus anthracis
3.4.22.B64 sortase D
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 Bacillus anthracis