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Information on EC 3.4.23.52 - preflagellin peptidase
for references in articles please use BRENDA:EC3.4.23.52
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.23 Aspartic endopeptidases
3.4.23.52 preflagellin peptidase
IUBMB Comments
An aspartic peptidase from Archaea but not bacteria. In peptidase family A24 (type IV prepilin peptidase family).
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 3.4.23.52
- preflagellins
- methanococcus
- flagellins
- prepilins
- voltae
-
flagellation
-
flak
- maripaludis
-
methanogen
- archaeon
-
flagella
- pilins
-
non-motile
-
glass
- glycans
-
sulfolobus
-
iv-like
-
unprocessed
-
n-linked
-
cotranscribed
-
pilus-like
-
non-flagellated
- preproteins
-
12-amino-acid
-
archaella
- synthesis
Reaction Schemes
showCleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-/- or Lys-Gly-/-, to release flagellin.
Synonyms
preflagellin peptidase, peptidase-like enzyme, spaseiii, signal peptidase iii, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EppA
FlaK
PibD
preflagellin peptidase
Prepilin peptidase
prepilin-like peptidase
RMVO00262
saci_0139
signal peptidase III
SPaseIII
type IV prepilin peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-/- or Lys-Gly-/-, to release flagellin.
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DUF361-containing proteins + H2O
?
Substrates: EppA specifically cleaves proteins with DUF361-like domains
Products: -
Products: -
?
FlaB2 + H2O
?
Substrates: -
Products: cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
Products: cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
?
MKGASGIGTLIVFIAMVLVAAV + H2O
MKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MKKGASGIGTLIVFIAMVLVAAV + H2O
MKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
pre-glucose-binding protein + H2O
glucose-binding protein + ?
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin + ?
Substrates: -
Products: -
Products: -
?
prepilin EpdE + H2O
pilin EpdE + EpdE signal peptide
-
Substrates: cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME
Products: -
Products: -
?
FlaB2 protein + H2O
?
-
Substrates: FlaB2 protein of Methanococcus voltae
Products: -
Products: -
?
FlaB2 protein + H2O
?
-
Substrates: FlaB2 protein of Methanococcus voltae
Products: -
Products: -
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
-
Substrates: -
Products: -
Products: -
?
prearchaellin + H2O
archaellin + ?
-
Substrates: -
Products: -
Products: -
?
precursor of flagellin + H2O
flagellin + ?
Substrates: processing of precursor of flagellin
Products: -
Products: -
?
precursor of flagellin + H2O
flagellin + ?
Substrates: the enzyme is responsible for processing of precursor of flagellin
Products: -
Products: -
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
Substrates: processing of precursor of glucose-binding protein
Products: -
Products: -
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
Substrates: the enzyme is responsible for the processing of precursor of glucose-binding protein
Products: -
Products: -
?
preflagellin + H2O
flagellin + ?
Substrates: -
Products: -
Products: -
?
preflagellin + H2O
flagellin + ?
Substrates: most efficient substrate
Products: -
Products: -
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
-
Substrates: preflagellin is MKIKEFMSNKKGASGIGTLIVFIAMVLVAAV, the enzyme cleaves the 12 amino acid N-terminal signal peptide from preflagellinFlaB2 between Gly and L-Ala
Products: -
Products: -
?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
-
Substrates: preflagellin is MKIKEFMSNKKGASGIGTLIVFIAMVLVAAV, the enzyme cleaves the 12 amino acid N-terminal signal peptide from preflagellinFlaB2 between Gly and L-Ala
Products: -
Products: -
?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
-
Substrates: preflagellin is MKIKEFMSNKKGASGIGTLIVFIAMVLVAAV
Products: -
Products: -
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
Substrates: cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
Products: -
Products: -
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
Substrates: cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
Products: -
Products: -
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
Substrates: cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
Products: -
Products: -
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
Substrates: cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
Products: -
Products: -
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
Substrates: cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
Products: -
Products: -
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
Substrates: cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
Products: -
Products: -
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
Substrates: cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
Products: -
Products: -
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
Substrates: cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
Products: -
Products: -
?
additional information
?
-
-
Substrates: FlaK processes preflagellins with a minimum signal peptide length of 5 amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with MKKGASGIGTLIVFIAMVLVAAV and MKGASGIGTLIVFIAMVLVAAV
Products: -
Products: -
?
additional information
?
-
-
Substrates: FlaK processes preflagellins with a minimum signal peptide length of 5 amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with MKKGASGIGTLIVFIAMVLVAAV and MKGASGIGTLIVFIAMVLVAAV
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is able to cleave type IV prepilin-like signal sequences with all amino acid combinations around the cleavage site that have been found in putative prepilin-like precursor proteins encoded by the Sulfolobus suolfataricus genome sequence
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FlaB2 + H2O
?
Substrates: -
Products: cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
Products: cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
?
precursor of flagellin + H2O
flagellin + ?
Substrates: the enzyme is responsible for processing of precursor of flagellin
Products: -
Products: -
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
Substrates: the enzyme is responsible for the processing of precursor of glucose-binding protein
Products: -
Products: -
?
prepilin EpdE + H2O
pilin EpdE + EpdE signal peptide
-
Substrates: cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME
Products: -
Products: -
?
prearchaellin + H2O
archaellin + ?
-
Substrates: -
Products: -
Products: -
?
preflagellin + H2O
flagellin + ?
Substrates: -
Products: -
Products: -
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
Substrates: cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
Products: -
Products: -
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
Substrates: cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
Products: -
Products: -
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
Substrates: cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
Products: -
Products: -
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
Substrates: cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
Products: -
Products: -
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
Substrates: cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
Products: -
Products: -
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
Substrates: cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
Products: -
Products: -
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
Substrates: cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
Products: -
Products: -
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
Substrates: cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
PilD is a zinc-binding protein. Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
KCl
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
KCl
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
KCl
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
KCl
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
KCl
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
additional information
wild type enzyme is not affected by 1,2-ethanedithiol dimethanesulfonate and dithiothreitol
-
additional information
-
wild type enzyme is not affected by 1,2-ethanedithiol dimethanesulfonate and dithiothreitol
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme contains a signal peptide
-
brenda
additional information
-
the enzyme contains a signal peptide
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
in Methanococcus maripaludis, the pilins have their own dedicated prepilin peptidase, EppA, which cleaves the signal peptide from pilins but not archaellins. This is in contrast to other studied Archaea which have a single prepilin peptidase-like enzyme, PibD, that cleaves all type IV pilin-like proteins, including archaellins, pilins and sugar binding proteins. Pilins in the organism are encoded by five genes, epdA-E. FlaK can only process archaellins and EppA only pilins
evolution
-
FlaK can only process archaellins and EppA only pilins
-
evolution
-
in Methanococcus maripaludis, the pilins have their own dedicated prepilin peptidase, EppA, which cleaves the signal peptide from pilins but not archaellins. This is in contrast to other studied Archaea which have a single prepilin peptidase-like enzyme, PibD, that cleaves all type IV pilin-like proteins, including archaellins, pilins and sugar binding proteins. Pilins in the organism are encoded by five genes, epdA-E. FlaK can only process archaellins and EppA only pilins
-
physiological function
-
the enzyme plays an essential role in flagellation
physiological function
-
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. Both archaella and archaeal type IV pili are assembled from structural proteins synthesized initially as preproteins with a class III (type IV pilin-like) signal peptide which is subsequently cleaved by a dedicated prepilin peptidase-like enzyme (signal peptidase III)
physiological function
-
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. The Epd pili of Methanococcus maripaludis are less numerous and thinner than archaella. Prepilin peptidase EppA cleaves the signal peptide from pilins but not archaellins
physiological function
type IV prepilin peptidase PibD processes flagellin/pilin precursors, that are essential for the biogenesis and function of the archaellum and other cell surface structures in Haloferax volcanii
physiological function
-
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. Both archaella and archaeal type IV pili are assembled from structural proteins synthesized initially as preproteins with a class III (type IV pilin-like) signal peptide which is subsequently cleaved by a dedicated prepilin peptidase-like enzyme (signal peptidase III)
-
physiological function
-
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. The Epd pili of Methanococcus maripaludis are less numerous and thinner than archaella. Prepilin peptidase EppA cleaves the signal peptide from pilins but not archaellins
-
physiological function
-
the enzyme plays an essential role in flagellation
-
physiological function
-
type IV prepilin peptidase PibD processes flagellin/pilin precursors, that are essential for the biogenesis and function of the archaellum and other cell surface structures in Haloferax volcanii
-
additional information
-
in Methanococcus maripaludis, the archaella are composed of three structural glycoproteins (the archaellins, FlaB1, FlaB2 and FlaB3) that are all modified at multiple positions with an N-linked tetrasaccharide
additional information
-
in Methanococcus maripaludis, the archaella are composed of three structural glycoproteins (the archaellins, FlaB1, FlaB2 and FlaB3) that are all modified at multiple positions with an N-linked tetrasaccharide
-
Show AA Sequence and Transmembrane Helices (104 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 15000-17000, recombinant EpdE from purified pili, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT