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Information on EC 3.4.23.52 - preflagellin peptidase
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EC Tree
3.4.23.52 preflagellin peptidaseSpecify your search results
Word Map
- 3.4.23.52
- preflagellins
- methanococcus
- flagellins
- voltae
- prepilins
-
flak
-
leader
-
flagellation
- maripaludis
- archaeon
-
methanogen
- pilins
-
flagella
-
non-motile
-
12-amino-acid
-
sulfolobus
-
cotranscribed
- glycans
-
non-flagellated
- proteases
-
unprocessed
-
n-linked
- preproteins
-
pilus-like
- synthesis
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
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.
Synonyms
EppA, FlaK, peptidase-like enzyme, PibD, preflagellin peptidase, Prepilin peptidase, prepilin-like peptidase, RMVO00262, saci_0139, 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
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
DUF361-containing proteins + H2O
?
EppA specifically cleaves proteins with DUF361-like domains
-
-
?
FlaB2 + H2O
?
-
cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
-
?
MKKGASGIGTLIVFIAMVLVAAV + H2O
MKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
pre-glucose-binding protein + H2O
glucose-binding protein + ?
-
-
-
-
?
prepilin EpdE + H2O
pilin EpdE + EpdE signal peptide
-
cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME
-
-
?
FlaB2 protein + H2O
?
-
FlaB2 protein of Methanococcus voltae
-
-
?
FlaB2 protein + H2O
?
-
FlaB2 protein of Methanococcus voltae
-
-
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
precursor of flagellin + H2O
flagellin + ?
processing of precursor of flagellin
-
?
precursor of flagellin + H2O
flagellin + ?
the enzyme is responsible for processing of precursor of flagellin
-
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
processing of precursor of glucose-binding protein
-
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
the enzyme is responsible for the processing of precursor of glucose-binding protein
-
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
-
preflagellin is MKIKEFMSNKKGASGIGTLIVFIAMVLVAAV, the enzyme cleaves the 12 amino acid N-terminal signal peptide from preflagellinFlaB2 between Gly and L-Ala
-
-
?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
-
preflagellin is MKIKEFMSNKKGASGIGTLIVFIAMVLVAAV, the enzyme cleaves the 12 amino acid N-terminal signal peptide from preflagellinFlaB2 between Gly and L-Ala
-
-
?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
-
preflagellin is MKIKEFMSNKKGASGIGTLIVFIAMVLVAAV
-
-
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
-
-
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
-
-
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
-
-
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
-
-
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
-
-
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
-
-
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
-
-
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
-
-
?
additional information
?
-
-
FlaK processes preflagellins with a minimum signal peptide length of 5 amino acids
-
-
-
additional information
?
-
-
no activity with MKKGASGIGTLIVFIAMVLVAAV and MKGASGIGTLIVFIAMVLVAAV
-
-
-
additional information
?
-
-
FlaK processes preflagellins with a minimum signal peptide length of 5 amino acids
-
-
-
additional information
?
-
-
no activity with MKKGASGIGTLIVFIAMVLVAAV and MKGASGIGTLIVFIAMVLVAAV
-
-
-
additional information
?
-
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
-
?
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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
FlaB2 + H2O
?
-
cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
-
?
precursor of flagellin + H2O
flagellin + ?
the enzyme is responsible for processing of precursor of flagellin
-
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
the enzyme is responsible for the processing of precursor of glucose-binding protein
-
?
prepilin EpdE + H2O
pilin EpdE + EpdE signal peptide
-
cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME
-
-
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
-
-
?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
-
cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE
-
-
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
-
-
?
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
-
cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE
-
-
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
-
-
?
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
-
cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD
-
-
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
-
-
?
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
-
cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE
-
-
?
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
wild type enzyme is not affected by 1,2-ethanedithiol dimethanesulfonate and dithiothreitol
-
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
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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
D4GY85
the enzyme contains a signal peptide
-
brenda
additional information
-
the enzyme contains a signal peptide
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
FlaK can only process archaellins and EppA only pilins; 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; 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
D4GY85
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); 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); 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
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
FLAK_METM6
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
230
4
26021
Swiss-Prot
FLAK_METMP
Methanococcus maripaludis (strain S2 / LL)
230
4
25915
Swiss-Prot
FLAK_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
341
4
36559
Swiss-Prot
FLAK_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
234
5
26294
Swiss-Prot
A0A150J2S7_9EURY
241
5
27163
TrEMBL
A0A1V5A1X6_9EURY
276
6
31450
TrEMBL
A0A075MT83_9ARCH
248
5
26623
TrEMBL
A0A1V6JI10_9EURY
264
6
28927
TrEMBL
A0A150JMX6_9EURY
241
5
27568
TrEMBL
Q18DH1_HALWD
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
345
5
38021
TrEMBL
A0A1V4YWE8_9EURY
294
8
33225
TrEMBL
A0A510NA43_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
314
5
33154
TrEMBL
A0A1V5TRI0_9ARCH
272
7
31419
TrEMBL
A0A1Q9NVR6_9ARCH
258
5
29617
TrEMBL
A0A564Q0C2_9EURY
235
6
26627
TrEMBL
B0R7I2_HALS3
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
314
5
33154
TrEMBL
A0A0P8A7T0_9EURY
253
5
29261
TrEMBL
A0A1V4TGI6_9EURY
293
7
32712
TrEMBL
A0A1V4ZCF1_9EURY
317
8
36036
TrEMBL
A0A087S7S5_9ARCH
231
5
25406
TrEMBL
A0A1U7EUR1_NATPD
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / NBRC 14720 / NCIMB 2260 / Gabara)
333
5
36047
TrEMBL
M1XZ62_NATM8
Natronomonas moolapensis (strain DSM 18674 / JCM 14361 / 8.8.11)
326
6
34928
TrEMBL
A0A1V5Z8Z4_9EURY
277
6
31177
TrEMBL
A0A1V4Y9Y5_9EURY
255
5
28799
TrEMBL
A0A1V4Y6R7_9EURY
255
5
28543
TrEMBL
A0A087RS16_9ARCH
231
5
25406
TrEMBL
A0A150IRW0_9EURY
241
5
27558
TrEMBL
G0LFY5_HALWC
Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23)
345
5
38063
TrEMBL
A0A1V4TK76_9EURY
293
8
32595
TrEMBL
A0A087S2T8_9ARCH
214
4
23817
TrEMBL
A0A1V6IM08_9EURY
241
5
27568
TrEMBL
A0A4D6GVT3_HALS9
Halobacterium salinarum (strain ATCC 33171 / DSM 3754 / JCM 8978 / NBRC 102687 / NCIMB 764 / 91-R6)
314
5
33154
TrEMBL
A0A062VB27_9EURY
248
5
27800
TrEMBL
A0A0A7LA08_9EURY
287
8
32596
TrEMBL
A0A150J863_9EURY
241
5
27403
TrEMBL
Q4JCB7_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
93
0
10996
TrEMBL
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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
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
EpdE is a glycoprotein with multiple sites occupied by an N-linked glycan
glycoprotein
-
EpdE is a glycoprotein with multiple sites occupied by an N-linked glycan
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 30% (w/v) PEG 300, 50 mM glycine (pH 9.5) and 100 mM NaCl
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D186A
-
the mutation does not affect the activity towards preflagellin FlaB2
D190A
-
the mutation does not affect the activity towards preflagellin FlaB2
D224A
-
the mutation does not affect the activity towards preflagellin FlaB2
D79E
-
the mutant restores preflagellin peptidase activity (despite a reduced amount of peptidase produced)
D186A
-
the mutation does not affect the activity towards preflagellin FlaB2
-
D190A
-
the mutation does not affect the activity towards preflagellin FlaB2
-
D157A
-
the activity level of the mutant is comparable to that of the wild type enzyme
D173A
-
the activity level of the mutant is comparable to that of the wild type enzyme
D180A
-
the activity level of the mutant is comparable to that of the wild type enzyme
D207N
-
the activity level of the mutant is comparable to that of the wild type enzyme
D30A
-
the activity level of the mutant is comparable to that of the wild type enzyme
A77G
activity level is comparable to that of the wild type enzyme under standard assay conditions
A77P
activity level is comparable to that of the wild type enzyme under standard assay conditions; cleavage activity is reduced
D185A
activity of the mutant enzyme is lower than activity of wild-type enzyme
D186A
activity level is comparable to that of the wild type enzyme under standard assay conditions
I22E
activity level is comparable to that of the wild type enzyme under standard assay conditions
K23A
activity level is comparable to that of the wild type enzyme under standard assay conditions
K24A
activity level is comparable to that of the wild type enzyme under standard assay conditions
L81A
activity level is comparable to that of the wild type enzyme under standard assay conditions
R25A
single mutant displays Aap pili even though no preopillin AapA-processing is observed
D186A
-
activity level is comparable to that of the wild type enzyme under standard assay conditions
-
L81A
-
activity level is comparable to that of the wild type enzyme under standard assay conditions
-
R25A
-
single mutant displays Aap pili even though no preopillin AapA-processing is observed
-
additional information
additional information
-
construction of deletion mutant strains DELTAeppA, DELTAeppADELTAaglB, and DELTAflakDELTAeppA. AglB is the oligosaccharyltransferase responsible for the terminal step in the N-linked glycosylation pathway. In the DELTAeppA mutant where the signal peptide is not be removed from the pilins, the proteins EpdE and EpdD migrate faster than the same proteins in wild-type cells, despite the fact the proteins are larger due to the additional signal peptide in the DELTAeppA strain. In the DELTAaglBDELTAeppA double mutant, the electrophoretic mobility of EpdE-FLAG and EpdD-FLAG is the same as it was in the DELTAeppA strain; construction of deletion mutant strains DELTAflak, DELTAflakDELTAaglB, and DELTAflakDELTAeppA. AglB is the oligosaccharyltransferase responsible for the terminal step in the N-linked glycosylation pathway
additional information
-
construction of deletion mutant strains DELTAeppA, DELTAeppADELTAaglB, and DELTAflakDELTAeppA. AglB is the oligosaccharyltransferase responsible for the terminal step in the N-linked glycosylation pathway. In the DELTAeppA mutant where the signal peptide is not be removed from the pilins, the proteins EpdE and EpdD migrate faster than the same proteins in wild-type cells, despite the fact the proteins are larger due to the additional signal peptide in the DELTAeppA strain. In the DELTAaglBDELTAeppA double mutant, the electrophoretic mobility of EpdE-FLAG and EpdD-FLAG is the same as it was in the DELTAeppA strain; construction of deletion mutant strains DELTAflak, DELTAflakDELTAaglB, and DELTAflakDELTAeppA. AglB is the oligosaccharyltransferase responsible for the terminal step in the N-linked glycosylation pathway
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Triton X-100
Triton X-100
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
Triton X-100
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
Triton X-100
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
Triton X-100
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
Triton X-100
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
Triton X-100
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crude membrane fraction
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a His-tagged version expressed in Escherichia coli; expressed in an Methanococcus maripaludis DELTAflaK strain and in Escherichia coli
-
expression in Escherichia coli
gene eppA, recombinant expression of C-terminally FLAG- or His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3); gene flak, recombinant expression of C-terminally FLAG- or His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
scaled-up synthesis of PilD, followed by solubilization in dodecyl-beta-D-maltoside and chromatography, leads to a pure enzyme that retains its known biochemical activities
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Albers, S.V.; Szabo, Z.; Driessen, A.J.M.
Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
J. Bacteriol.
185
3918-3925
2003
Saccharolobus solfataricus (Q6IFS8)
brenda
Szabo, Z.; Albers, S.V.; Driessen, A.J.
Active-site residues in the type IV prepilin peptidase homologue PibD from the archaeon Sulfolobus solfataricus
J. Bacteriol.
188
1437-1443
2006
Saccharolobus solfataricus (Q6IFS8)
brenda
Szabo, Z.; Stahl, A.O.; Albers, S.V.; Kissinger, J.C.; Driessen, A.J.; Pohlschroeder, M.
Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases
J. Bacteriol.
189
772-778
2007
Methanococcus maripaludis, Methanococcus maripaludis (Q6LZR9)
brenda
Ng, S.Y.; VanDyke, D.J.; Chaban, B.; Wu, J.; Nosaka, Y.; Aizawa, S.; Jarrell, K.F.
Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD
J. Bacteriol.
191
6732-6740
2009
Methanococcus maripaludis, Methanococcus voltae, Saccharolobus solfataricus
brenda
Bardy, S.L.; Jarrell, K.F.
FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity
FEMS Microbiol. Lett.
208
53-59
2002
Methanococcus maripaludis, Methanococcus maripaludis (Q6LZR9)
brenda
Correia, J.D.; Jarrell, K.F.
Posttranslational processing of Methanococcus voltae preflagellin by preflagellin peptidases of M. voltae and other methanogens
J. Bacteriol.
182
855-858
2000
Methanocaldococcus jannaschii, Methanococcus maripaludis, Methanococcus vannielii, Methanococcus voltae, Methanothermococcus thermolithotrophicus, no activity in Methanococcus igneus, no activity in Methanoculleus marisnigri, no activity in Methanogenium cariaci, Pseudomonas aeruginosa
brenda
Bardy, S.L.; Jarrell, K.F.
Cleavage of preflagellins by an aspartic acid signal peptidase is essential for flagellation in the archaeon Methanococcus voltae
Mol. Microbiol.
50
1339-1347
2003
Methanococcus voltae, Methanococcus voltae PS
brenda
Hu, J.; Xue, Y.; Lee, S.; Ha, Y.
The crystal structure of GXGD membrane protease FlaK
Nature
475
528-531
2011
Methanococcus maripaludis (A9A677), Methanococcus maripaludis
brenda
Henche, A.L.; van Wolferen, M.; Ghosh, A.; Albers, S.V.
Dissection of key determinants of cleavage activity in signal peptidase III (SPaseIII) PibD
Extremophiles
18
905-913
2014
Sulfolobus acidocaldarius (Q4JCB7), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q4JCB7)
brenda
Aly, K.A.; Beebe, E.T.; Chan, C.H.; Goren, M.A.; Sepulveda, C.; Makino, S.; Fox, B.G.; Forest, K.T.
Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD
MicrobiologyOpen
2
94-104
2013
Methanococcus voltae (Q8NKW5)
brenda
Gimenez, M.; Cerletti, M.; De Castro, R.
Archaeal membrane-associated proteases Insights on Haloferax volcanii and other haloarchaea
Front. Microbiol.
6
39
2015
Haloferax volcanii (D4GY85), Haloferax volcanii ATCC 29605 (D4GY85)
brenda
Nair, D.; Jarrell, K.
Pilin processing follows a different temporal route than that of archaellins in Methanococcus maripaludis
Life
5
85-101
2015
Methanococcus maripaludis, Methanococcus maripaludis Mm900
brenda
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