Information on EC 3.4.22.B64 - sortase D

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B64
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
sortase D
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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.
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain NCTC13129
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Manually annotated by BRENDA team
strain NCTC13129
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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sortase D links major pilin protein BcpA and minor tip pilin BcpB together. The enzyme cleaves related sorting signals within BcpA (LPVTG) and BcpB (IPNTG), and catalyses a transpeptidation that joins the threonine residues in each signal to the side-chain of Lys162 in BcpA (located within a pilin motif)
SUBSTRATE
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
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show the reaction diagram
pilin protein BcpA + H2O
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show the reaction diagram
pilin protein BcpB + H2O
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show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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show the reaction diagram
pilin protein BcpB + H2O
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C207A
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although sortase C207A is expressed at the same level as the wild-type enzyme, the mutant was unable to cleave IsdX1SS-GST substrate