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Literature summary extracted from

  • Budzik, J.M.; Marraffini, L.A.; Souda, P.; Whitelegge, J.P.; Faull, K.F.; Schneewind, O.
    Amide bonds assemble pili on the surface of bacilli (2008), Proc. Natl. Acad. Sci. USA, 105, 10215-10220.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.B64 major pilin protein BcpA precursor + H2O Bacillus cereus BcpA cleavage by SrtD leads to the assembly of pili, fibrous structures formed by intermolecular amide bonds between the C-terminal threonine of cleaved sorting signals (Thr522) and the conserved lysine residue of the YPKN motif (Lys162). The acyl enzyme of SrtD can be viewed as an assembly platform for the capture of polymerized pili via thioester linked intermediates with the C-terminal threonine of the last pilin subunit ?
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Organism

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

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.B64 major pilin protein BcpA precursor + H2O BcpA cleavage by SrtD leads to the assembly of pili, fibrous structures formed by intermolecular amide bonds between the C-terminal threonine of cleaved sorting signals (Thr522) and the conserved lysine residue of the YPKN motif (Lys162). The acyl enzyme of SrtD can be viewed as an assembly platform for the capture of polymerized pili via thioester linked intermediates with the C-terminal threonine of the last pilin subunit Bacillus cereus ?
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3.4.22.B64 major pilin protein BcpA precursor + H2O sortase D cleaves the BcpA precursor between the threonine and the glycine residues of its LPXTG sorting signal and catalyzes formation of an amide bond between threonine of the sorting signal and lysine in the YPKN motif of another BcpA subunit. BcpA cleavage by SrtD leads to the assembly of pili, fibrous structures formed by intermolecular amide bonds between the C-terminal threonine of cleaved sorting signals (Thr522) and the conserved lysine residue of the YPKN motif (Lys162). The acyl enzyme of SrtD can be viewed as an assembly platform for the capture of polymerized pili via thioester linked intermediates with the C-terminal threonine of the last pilin subunit Bacillus cereus ?
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