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3.4.22.B64: sortase D

This is an abbreviated version!
For detailed information about sortase D, go to the full flat file.

Word Map on EC 3.4.22.B64

Reaction

Sortase D cleaves major pilin protein (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. 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. =

Synonyms

CPE0222, pilin-specific sortase D, pilus-associated sortase D, sortase D, sortase SrtD, SrtD

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B64 sortase D

Natural Substrates Products

Natural Substrates Products on EC 3.4.22.B64 - sortase D

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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
major pilin protein BcpA precursor + H2O
?
show the reaction diagram
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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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?
pilin protein BcpA + H2O
?
show the reaction diagram
pilin protein BcpB + H2O
?
show the reaction diagram
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Bacillus cereus and other Gram-positive bacteria elaborate pili via a sortase D-catalyzed transpeptidation mechanism from major and minor pilin precursor substrates. After cleavage of the LPXTG sorting signal of the major pilin, BcpA, sortase D forms an amide bond between the C-terminal threonine and the amino group of lysine within the YPKN motif of another BcpA subunit. The IPNTG sorting signal of BcpB, the minor pilin, is cleaved by sortase D but not by sortase A. The C-terminal threonine of BcpB is amide-linked to the YPKN motif of BcpA, thereby positioning BcpB at the tip of pili
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?
additional information
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