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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 + ?
-
-
-
?
prearchaellin + H2O
archaellin + ?
precursor of flagellin + H2O
flagellin + ?
precursor of glucose-binding protein + H2O
glucose-binding protein + ?
preflagellin + H2O
flagellin + ?
preflagellin FlaB1 + H2O
flagellin FlaB1 + ?
preflagellin FlaB2 + H2O
flagellin + ?
-
-
-
?
preflagellin FlaB2 + H2O
flagellin FlaB2 + ?
preflagellin FlaB2 + H2O
MKIKEFMSNKKG + flagellin
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
prepilin EpdE + H2O
pilin EpdE + EpdE signal peptide
-
cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME
-
-
?
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
-
-
-
-
?
prearchaellin + H2O
archaellin + ?
-
-
-
-
?
prearchaellin + H2O
archaellin + ?
-
-
-
-
?
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 + H2O
flagellin + ?
-
-
-
?
preflagellin + H2O
flagellin + ?
-
-
-
?
preflagellin + H2O
flagellin + ?
most efficient substrate
-
-
?
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 + H2O
pilin + ?
-
-
-
?
prepilin + H2O
pilin + ?
-
-
-
?
prepilin AapA + H2O
?
-
-
-
?
prepilin AapA + H2O
?
-
-
-
?
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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FlaB2 + H2O
?
-
cosynthesis of of FlaK with its full-length substrate, FlaB2, leads to complete cleavage of the substrate signal peptides
-
?
FlaB2 protein + H2O
?
-
-
-
-
?
prearchaellin + H2O
archaellin + ?
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
-
?
preflagellin + H2O
flagellin + ?
prepilin EpdA + H2O
pilin EpdA + EpdA signal peptide
prepilin EpdB + H2O
pilin EpdB + EpdB signal peptide
prepilin EpdC + H2O
pilin EpdC + EpdC signal peptide
prepilin EpdD + H2O
pilin EpdD + EpdD signal peptide
prepilin EpdE + H2O
pilin EpdE + EpdE signal peptide
-
cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME
-
-
?
prearchaellin + H2O
archaellin + ?
-
-
-
-
?
prearchaellin + H2O
archaellin + ?
-
-
-
-
?
preflagellin + H2O
flagellin + ?
-
-
-
?
preflagellin + H2O
flagellin + ?
-
-
-
?
prepilin + H2O
pilin + ?
-
-
-
?
prepilin + H2O
pilin + ?
-
-
-
?
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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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
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
-
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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
-
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
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
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
-
A77P
activity level is comparable to that of the wild type enzyme under standard assay conditions
A77P
cleavage activity is reduced
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
additional information
-
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
-
additional information
-
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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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)
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Szabo, Z.; Stahl, A.O.; Albers, S.V.; Kissinger, J.C.; Driessen, A.J.; Pohlschroeder, M.
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772-778
2007
Methanococcus maripaludis (Q6LZR9), Methanococcus maripaludis
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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.
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6732-6740
2009
Methanococcus maripaludis, Methanococcus voltae, Saccharolobus solfataricus
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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 (Q6LZR9), Methanococcus maripaludis
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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, Methanothermococcus thermolithotrophicus, Methanococcus vannielii, Methanococcus voltae, Pseudomonas aeruginosa, no activity in Methanococcus igneus, no activity in Methanoculleus marisnigri, no activity in Methanogenium cariaci
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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
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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