We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 3.4.23.52 - preflagellin peptidase for references in articles please use BRENDA:EC3.4.23.52Word Map on EC 3.4.23.52
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EppA
-
-
FlaK
-
-
PibD
-
preflagellin peptidase
-
-
preflagellin peptidase
-
-
preflagellin peptidase
-
-
prepilin-like peptidase
-
-
prepilin-like peptidase
-
-
RMVO00262
-
recombinant enzyme
RMVO00262
-
recombinant enzyme
-
saci_0139
locus name
signal peptidase III
-
SPaseIII
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
no activity in Methanococcus igneus
-
-
-
brenda
no activity in Methanoculleus marisnigri
-
-
-
brenda
no activity in Methanogenium cariaci
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
SwissProt
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
-
the enzyme plays an essential role in flagellation
physiological function
-
the enzyme plays an essential role in flagellation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
?
MEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MEFMSNKKG + ASGIGTLIVFIAMVLVAAV
MFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MFMSNKKG + ASGIGTLIVFIAMVLVAAV
MKEFMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MKEFMSNKKG + ASGIGTLIVFIAMVLVAAV
MKGASGIGTLIVFIAMVLVAAV + H2O
MKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MKKGASGIGTLIVFIAMVLVAAV + H2O
MKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MMSNKKGASGIGTLIVFIAMVLVAAV + H2O
MMSNKKG + ASGIGTLIVFIAMVLVAAV
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + ASGIGTLIVFIAMVLVAAV
pre-glucose-binding protein + H2O
glucose-binding protein + ?
-
-
-
-
?
precursor of flagellin + H2O
flagellin + ?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
preflagellin + H2O
flagellin + ?
-
most efficient substrate
-
-
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
preflagellin FlaB2 + H2O
flagellin + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
additional information
?
-
FlaB2 protein + H2O
?
-
FlaB2 protein of Methanococcus voltae
-
-
?
FlaB2 protein + H2O
?
-
-
-
-
?
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
-
-
-
-
?
MNKKGASGIGTLIVFIAMVLVAAV + H2O
MNKKG + ASGIGTLIVFIAMVLVAAV
-
-
-
-
?
MSNKKGASGIGTLIVFIAMVLVAAV + H2O
MSNKKG + 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 FlaB1 + H2O
flagellin FlaB1 + ?
-
-
-
-
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
-
-
-
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
-
-
-
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
-
-
-
?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
-
-
-
-
?
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 AapA + H2O
?
-
-
-
?
prepilin AapA + H2O
?
-
-
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FlaB2 + H2O
?
Q8NKW5
-
cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
-
?
FlaB2 protein + H2O
?
-
-
-
-
?
precursor of flagellin + H2O
flagellin + ?
Q6IFS8
the enzyme is responsible for processing of precursor of flagellin
-
?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
Q6IFS8
the enzyme is responsible for the processing of precursor of glucose-binding protein
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8.5
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
integral membrane protein
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
25900
-
x * 25900, calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 25900, calculated from amino acid sequence
?
-
x * 25900, calculated from amino acid sequence
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
sitting drop vapor diffusion method, using 30% (w/v) PEG 300, 50 mM glycine (pH 9.5) and 100 mM NaCl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metal-affinity column chromatography and gel filtration
crude membrane fraction
-
crude membrane fraction
-
crude membrane fraction
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a His-tagged version expressed in Escherichia coli; expressed in an Methanococcus maripaludis DELTAflaK strain and in Escherichia coli
-
expressed in an Methanococcus maripaludis DELTAflaK strain
-
expressed in BL21(DE3)/pLysS membranes
-
expressed in Escherichia coli K113 cell membranes
-
expressed in Escherichia coli Rosetta 2 (DE3) cells
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E25C/I206C
the mutant is proteolytically active
D186A
-
the mutation does not affect the activity towards preflagellin FlaB2
D18E
-
the mutation results in an apparently unstable protein
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
-
A77E
mutant enzyme shows no processing of prepillin AapA
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
D21A
mutant enzyme shows no processing of prepillin AapA
D78A
mutant enzyme shows no processing of prepillin AapA
G75E
mutant enzyme shows no processing of prepillin AapA
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
W32A
mutation results in reduced activity
D186A
-
activity level is comparable to that of the wild type enzyme under standard assay conditions
-
D21A
-
mutant enzyme shows no processing of prepillin AapA
-
D78A
-
mutant enzyme shows no processing of prepillin AapA
-
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
-
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
D187A
-
the mutant shows an apparent reduction in activity
D187A/D188A
-
the mutant does not cleave preflagellin
D188A
-
the mutant shows about wild type activity
D207N
-
the activity level of the mutant is comparable to that of the wild type enzyme
D23A
-
the mutant does not cleave preflagellin
D30A
-
the activity level of the mutant is comparable to that of the wild type enzyme
D80A
-
the mutant does not cleave preflagellin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FLAK_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
341
36559
Swiss-Prot
FLAK_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
234
26294
Swiss-Prot
FLAK_METM6
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
230
26021
Swiss-Prot
FLAK_METMP
Methanococcus maripaludis (strain S2 / LL)
230
25915
Swiss-Prot
FLAK_METVO
233
25888
Swiss-Prot
A0A0A7LA08_9EURY
287
32596
TrEMBL
A0A075MT83_9ARCH
248
26623
TrEMBL
M1XZ62_NATM8
Natronomonas moolapensis (strain DSM 18674 / JCM 14361 / 8.8.11)
326
34928
TrEMBL
A0A1V6IM08_9EURY
241
27568
TrEMBL
A0A1V4Y6R7_9EURY
255
28543
TrEMBL
B0R7I2_HALS3
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
314
33154
TrEMBL
A0A087S7S5_9ARCH
231
25406
TrEMBL
A0A150JBY0_9EURY
241
27568
TrEMBL
Q18DH1_HALWD
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
345
38021
TrEMBL
G0LFY5_HALWC
Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23)
345
38063
TrEMBL
A0A1V6JI10_9EURY
264
28927
TrEMBL
A0A075WFC1_ARCFL
240
27171
TrEMBL
A0A087RS16_9ARCH
231
25406
TrEMBL
A0A1Q9NVR6_9ARCH
258
29617
TrEMBL
A0A1V4TGI6_9EURY
293
32712
TrEMBL
A0A062VB27_9EURY
248
27800
TrEMBL
A0A1V5TRI0_9ARCH
272
31419
TrEMBL
A0A150J863_9EURY
241
27403
TrEMBL
A0A087S2T8_9ARCH
214
23817
TrEMBL
A0A150IKJ4_9EURY
241
27558
TrEMBL
A0A150IRW0_9EURY
241
27558
TrEMBL
A0A1V4YWE8_9EURY
294
33225
TrEMBL
A0A1V4Y9Y5_9EURY
255
28799
TrEMBL
A0A1V5QPX7_9ARCH
370
41311
TrEMBL
A0A0K1E1A6_9CREN
193
21134
TrEMBL
A0A1V4ZCF1_9EURY
317
36036
TrEMBL
A0A150JFY9_9EURY
241
27568
TrEMBL
A0A150JMX6_9EURY
241
27568
TrEMBL
V6DP53_9EURY
335
37132
TrEMBL
A0A1V4TK76_9EURY
293
32595
TrEMBL
A0A0P8A7T0_9EURY
253
29261
TrEMBL
A0A1V5Z8Z4_9EURY
277
31177
TrEMBL
A0A2P5K178_9EURY
255
29139
TrEMBL
A0A1U7EUR1_NATPD
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / NBRC 14720 / NCIMB 2260 / Gabara)
333
36047
TrEMBL
A0A0B3AVC4_9ARCH
276
31008
TrEMBL
A0A0F7IGV4_9EURY
246
27972
TrEMBL
A0A0B5HU84_ARCG5
372
41007
TrEMBL
A0A150J2S7_9EURY
241
27163
TrEMBL
Q6IFS8_SULSF
236
27498
TrEMBL
Q4JCB7_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
93
10996
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Sulfolobus 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
Sulfolobus 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, Sulfolobus 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
html completed