Information on EC 3.4.23.43 - prepilin peptidase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.4.23.43
-
RECOMMENDED NAME
GeneOntology No.
prepilin peptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
typically cleaves a -Gly-/-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
202833-59-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene tadV of the tad locus
-
-
Manually annotated by BRENDA team
gene comC
-
-
Manually annotated by BRENDA team
gene outO
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Legionella pneumoniae
gene pilD
-
-
Manually annotated by BRENDA team
gene pilD
-
-
Manually annotated by BRENDA team
pilD mutant strain
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene xpsO
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Flp1 prepilin + H2O
Flp1 pilin + Flp1 prepilin leader peptide
show the reaction diagram
Msh prepilin + H2O
?
show the reaction diagram
-
-
-
-
?
pilin type-IV precursor + H2O
pilin type-IV
show the reaction diagram
-
-
-
-
?
PilS2 + H2O
?
show the reaction diagram
-
precursor of the major pilus subunit
-
-
?
preflagellin + H2O
flagellin + preflagellin leader peptide
show the reaction diagram
-
-
-
?
prepilin PilA + H2O
?
show the reaction diagram
prepilin type IV + H2O
pilin type IV + leader peptide
show the reaction diagram
prepilin type IV + H2O
pilin type IV + prepilin type IV leader peptide
show the reaction diagram
prePulG + H2O
?
show the reaction diagram
-
processing of proteins which are required for pullulanase secretion
-
-
?
T2S prepseudopilin + H2O
?
show the reaction diagram
-
-
-
-
?
TadE prepseudopilin + H2O
TadE pseudopilin + TadE prepseudopilin leader peptide
show the reaction diagram
TadF prepseudopilin + H2O
TadF pseudopilin + TadF prepseudopilin leader peptide
show the reaction diagram
TcpA + H2O
?
show the reaction diagram
-
prepilin-containing membrane preparation
-
-
?
type IV Flp1 prepilin + H2O
type IV Flp1 pilin + type IV Flp1 prepilin leader peptide
show the reaction diagram
type IV prepilin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Flp1 prepilin + H2O
Flp1 pilin + Flp1 prepilin leader peptide
show the reaction diagram
-
the enzyme is required for maturation of the Flp1 pilin and TadE and TadF pseudopilins which are essential for adhesion of the bacterium to surfaces and formation of strong biofilms
-
-
?
preflagellin + H2O
flagellin + preflagellin leader peptide
show the reaction diagram
Q6IFS8
-
-
-
?
prepilin PilA + H2O
?
show the reaction diagram
prepilin type IV + H2O
pilin type IV + leader peptide
show the reaction diagram
-
prepilin maturation is required for extracellular protein secretion, and competence state and DNA uptake, overview
-
-
?
prepilin type IV + H2O
pilin type IV + prepilin type IV leader peptide
show the reaction diagram
TadE prepseudopilin + H2O
TadE pseudopilin + TadE prepseudopilin leader peptide
show the reaction diagram
-
the enzyme is required for maturation of the Flp1 pilin and TadE and TadF pilin-like proteins which are essential for adhesion of the bacterium to surfaces and formation of strong biofilms
-
-
?
TadF prepseudopilin + H2O
TadF pseudopilin + TadF prepseudopilin leader peptide
show the reaction diagram
-
the enzyme is required for maturation of the Flp1 pilin and TadE and TadF pilin-like proteins which are essential for adhesion of the bacterium to surfaces and formation of strong biofilms
-
-
?
type IV Flp1 prepilin + H2O
type IV Flp1 pilin + type IV Flp1 prepilin leader peptide
show the reaction diagram
-
maturation of pilin type IV, the enzyme is involved in the assembly of type IVb pili required for motility and attachment, overview
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride/glycinamide
-
inhibitor for acid proteases
iodoacetamide
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
p-Chloromercuriphenylsulfonate
-
-
additional information
-
no inhibition by inhibitors of cysteine proteases, serine proteases, metallopeptidases, aminopeptidases, aspartic proteases
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
prepilin type IV
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
prepilin type IV
Pseudomonas aeruginosa
-
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from membrane by detergent solubilization and immunoaffinity chromatography
-
native TadV partially from Actinobacillus actinomycetemcomitans strains
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recombinant enzyme from Escherichia coli inner membrane vesicles
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli in inner membrane vesicles
gene fppA, DNA and amino acid sequence determination and analysis, expression of wild-type and mutants in strain PAO1, method optimization
-
gene pilU, expression of wild-type and mutant enzymes from plasmid R64 in strain DH5alpha and BL21(DE3)
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gene tadV, DNA and amino acid sequence determination and analysis, functional expression of wild-type enzyme in Escherichia coli strain BL21(DE3)
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pilD mutants with excretion defect, expression in Escherichia coli DH5alpha
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A129V
-
random mutagenesis, DNA sequence determination, inactive mutant
A92V
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
C170R
-
random mutagenesis, DNA sequence determination, inactive mutant
C200R
-
random mutagenesis, DNA sequence determination, inactive mutant
D151N
-
random mutagenesis, DNA sequence determination, inactive mutant
D91N
-
random mutagenesis, DNA sequence determination, inactive mutant
E125G
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
F101L
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
F30Y
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
G95D
-
random mutagenesis, DNA sequence determination, inactive mutant
H76L
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
H76R
-
random mutagenesis, DNA sequence determination, inactive mutant
I114N
-
random mutagenesis, DNA sequence determination, inactive mutant
I23T
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
I24V
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
K138R
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
K188R
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
K191E
-
random mutagenesis, DNA sequence determination, inactive mutant
K45R
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
L136P
-
random mutagenesis, DNA sequence determination, inactive mutant
L66S
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
L81P
-
random mutagenesis, DNA sequence determination, inactive mutant
L93P
-
random mutagenesis, DNA sequence determination, inactive mutant
L96S
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
L97I
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
L97S
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
M110R
-
random mutagenesis, DNA sequence determination, inactive mutant
M87K
-
random mutagenesis, DNA sequence determination, inactive mutant
N210D
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
Q86R
-
random mutagenesis, DNA sequence determination, inactive mutant
S112P
-
random mutagenesis, DNA sequence determination, inactive mutant
S82L
-
random mutagenesis, DNA sequence determination, inactive mutant
T102A
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
T128N
-
random mutagenesis, DNA sequence determination, inactive mutant
V132D
-
random mutagenesis, DNA sequence determination, inactive mutant
V140D
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
W153R
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
W161R
-
random mutagenesis, DNA sequence determination, inactive mutant
W169G
-
random mutagenesis, DNA sequence determination, reduced activity compared to the wild-type enzyme
W185R
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
W55R
-
random mutagenesis, DNA sequence determination, inactive mutant
Y212C
-
random mutagenesis, DNA sequence determination, highly reduced activity compared to the wild-type enzyme
D17A
-
site-directed mutagenesis, inactive mutant
D17A/D78A
-
site-directed mutagenesis, inactive mutant
D78A
-
site-directed mutagenesis, inactive mutant
D157A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D173A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D180A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D187A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D187A/D188A
site-directed mutagenesis, inactive mutant
D188A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D207N
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D23A
site-directed mutagenesis, inactive mutant
D30A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D80A
site-directed mutagenesis, inactive mutant
D80E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C51A
-
activity identical to wild-type
C73A
-
activity identical to wild-type
C76A
-
activity identical to wild-type
D125A
-
no peptidase activity
D125E
-
partial peptidase activity
D125N
-
no peptidase activity
D183N
-
activity identical to wild-type
D189E
-
partial peptidase activity
D189N
-
no peptidase activity
D198A
-
no peptidase activity
E88A
-
activity identical to wild-type
K191A
-
activity identical to wild-type
S172A
-
activity identical to wild-type
S18A
-
activity identical to wild-type
S46A
-
activity identical to wild-type
S65A
-
activity identical to wild-type
S81L
-
activity identical to wild-type
additional information
-
effects of mutations on membrane topology of mutants, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the pathogenicity island PAPI-1 may have evolved by acquisition of a conjugation system but because of its dependence on an essential chromosomal determinant, its transfer is restricted to Pseudomonas aeruginosa or other species capable of providing a functional prepilin peptidase
synthesis
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