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Information on EC 3.4.22.B64 - sortase D
for references in articles please use BRENDA:EC3.4.22.B64preliminary BRENDA-supplied EC number
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EC Tree
3.4.22.B64 sortase DSpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
sortase d, sortase srtd, pilin-specific sortase d, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPE0222
SrtD
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REACTION
REACTION DIAGRAM
COMMENTARY
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.
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-
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-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abeta1-16-LPQTGS + sortase D
?
first 16 aminoacid residues of the amyloid-beta peptide fused at the C-terminus with LPQTGS sorting motif
-
-
?
Abeta1-16-LPQTGS + sortase D
?
first 16 aminoacid residues of the amyloid-beta peptide fused at the C-terminus with LPQTGS sorting motif
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
pilin protein BcpA + H2O
?
-
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
-
-
?
pilin protein BcpB + H2O
?
-
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
-
-
?
pilin protein BcpB + H2O
?
-
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
-
-
?
additional information
?
-
enzyme shows a significant preference for the LPQTGS sorting motif over LPETG, LPNTGS, or LAETG sorting motifs
-
-
?
additional information
?
-
-
enzyme shows a significant preference for the LPQTGS sorting motif over LPETG, LPNTGS, or LAETG sorting motifs
-
-
?
additional information
?
-
enzyme shows a significant preference for the LPQTGS sorting motif over LPETG, LPNTGS, or LAETG sorting motifs
-
-
?
additional information
?
-
-
Corynebacterium diphtheriae SpaA pili are composed of three pilin subunits, SpaA, SpaB and SpaC. SpaA, the major pilin protein, is distributed uniformly along the pilus shaft, whereas SpaB is observed at regular intervals, and SpaC seems to be positioned at the pilus tip. Deletion of sortase gene srtD does not affected SpaA pilus assembly, polymerization of SpaA precursor into high-molecular-weight species or polymerization of SpaB into SpaBHMW complexes. When the main fimbrial subunit of Actinomyces naeslundii type I fimbriae, FimA, is expressed in Corynebacterium diphtheriae, FimA is polymerized to form short fibres. Although Corynebacterium diphtheriae does not depend on other actinomycetal genes for FimA polymerization, this process involves the pilin motif and the sorting signal of FimA as well as corynebacterial sortase D
-
-
?
additional information
?
-
-
Corynebacterium diphtheriae SpaA pili are composed of three pilin subunits, SpaA, SpaB and SpaC. SpaA, the major pilin protein, is distributed uniformly along the pilus shaft, whereas SpaB is observed at regular intervals, and SpaC seems to be positioned at the pilus tip. Deletion of sortase gene srtD does not affected SpaA pilus assembly, polymerization of SpaA precursor into high-molecular-weight species or polymerization of SpaB into SpaBHMW complexes. When the main fimbrial subunit of Actinomyces naeslundii type I fimbriae, FimA, is expressed in Corynebacterium diphtheriae, FimA is polymerized to form short fibres. Although Corynebacterium diphtheriae does not depend on other actinomycetal genes for FimA polymerization, this process involves the pilin motif and the sorting signal of FimA as well as corynebacterial sortase D
-
-
?
additional information
?
-
-
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. SrtD does not act as a pilus subunit polymerase, but instead is required for wild-type focal presentation of the pilus at the cell surface
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
pilin protein BcpB + H2O
?
-
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
-
-
?
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
-
-
?
pilin protein BcpA + H2O
?
-
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
-
-
?
additional information
?
-
-
Corynebacterium diphtheriae SpaA pili are composed of three pilin subunits, SpaA, SpaB and SpaC. SpaA, the major pilin protein, is distributed uniformly along the pilus shaft, whereas SpaB is observed at regular intervals, and SpaC seems to be positioned at the pilus tip. Deletion of sortase gene srtD does not affected SpaA pilus assembly, polymerization of SpaA precursor into high-molecular-weight species or polymerization of SpaB into SpaBHMW complexes. When the main fimbrial subunit of Actinomyces naeslundii type I fimbriae, FimA, is expressed in Corynebacterium diphtheriae, FimA is polymerized to form short fibres. Although Corynebacterium diphtheriae does not depend on other actinomycetal genes for FimA polymerization, this process involves the pilin motif and the sorting signal of FimA as well as corynebacterial sortase D
-
-
?
additional information
?
-
-
Corynebacterium diphtheriae SpaA pili are composed of three pilin subunits, SpaA, SpaB and SpaC. SpaA, the major pilin protein, is distributed uniformly along the pilus shaft, whereas SpaB is observed at regular intervals, and SpaC seems to be positioned at the pilus tip. Deletion of sortase gene srtD does not affected SpaA pilus assembly, polymerization of SpaA precursor into high-molecular-weight species or polymerization of SpaB into SpaBHMW complexes. When the main fimbrial subunit of Actinomyces naeslundii type I fimbriae, FimA, is expressed in Corynebacterium diphtheriae, FimA is polymerized to form short fibres. Although Corynebacterium diphtheriae does not depend on other actinomycetal genes for FimA polymerization, this process involves the pilin motif and the sorting signal of FimA as well as corynebacterial sortase D
-
-
?
additional information
?
-
-
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. SrtD does not act as a pilus subunit polymerase, but instead is required for wild-type focal presentation of the pilus at the cell surface
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Foodborne Diseases
Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase.
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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)
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q8XNW0_CLOPE
Clostridium perfringens (strain 13 / Type A)
187
0
20996
TrEMBL
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C207A
-
although sortase C207A is expressed at the same level as the wild-type enzyme, the mutant was unable to cleave IsdX1SS-GST substrate
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ton-That, H.; Marraffini, L.A.; Schneewind, O.
Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae
Mol. Microbiol.
53
251-261
2004
Corynebacterium diphtheriae, Corynebacterium diphtheriae NCTC13129
brenda
Budzik, J.M.
Oh, S.Y.; Schneewind, O.: Cell wall anchor structure of BcpA pili in Bacillus anthracis
J. Biol. Chem.
283
36676-3686
2008
Bacillus anthracis
brenda
Budzik, J.M.; Oh, S.Y.
Schneewind, O.: Sortase D forms the covalent bond that links BcpB to the tip of Bacillus cereus pili
J. Biol. Chem.
284
12989-12997
2009
Bacillus cereus
brenda
Flker, S.; Nelson, A.L.; Morfeldt, E.; Jonas, K.; Hultenby, K.; Ries, J.; Melefors, O.; Normark, S.; Henriques-Normark, B.
Sortase-mediated assembly and surface topology of adhesive pneumococcal pili
Mol. Microbiol.
70
595-607
2008
Streptococcus pneumoniae
brenda
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
Proc. Natl. Acad. Sci. USA
105
10215-10220
2008
Bacillus cereus
brenda
Neiers, F.; Madhurantakam, C.; Faelker, S.; Manzano, C.; Dessen, A.; Normark, S.; Henriques-Normark, B.; Achour, A.
Two crystal structures of pneumococcal pilus sortase C provide novel insights into catalysis and substrate specificity
J. Mol. Biol.
393
704-716
2009
Streptococcus pneumoniae
brenda
Spirig, T.; Weiner, E.; Clubb, R.
Sortase enzymes in Gram-positive bacteria
Mol. Microbiol.
82
1044-1059
2011
Bacillus cereus
brenda
Suryadinata, R.; Seabrook, S.A.; Adams, T.E.; Nuttall, S.D.; Peat, T.S.
Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase
Acta Crystallogr. Sect. D
71
1505-1513
2015
Clostridium perfringens (Q8XNW0), Clostridium perfringens, Clostridium perfringens 13 (Q8XNW0)
brenda
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Release 2023.1 (January 2023)
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