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Information on EC 3.4.23.43 - prepilin peptidase and Organism(s) Pseudomonas aeruginosa and UniProt Accession P22610

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.43 prepilin peptidase
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: P22610 not found.
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
prepilin peptidase, type iv prepilin peptidase, type 4 prepilin peptidase, type iv prepilin-like peptidase, tadv protein, prepilin peptidase pild/xcpa, pulo prepilin peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Prepilin peptidase
-
Pilin leader peptidase
-
-
-
-
Prepilin peptidase
-
-
-
-
prepilin peptidase PilD/XcpA
-
-
-
-
proepilin peptidase PulO
-
-
-
-
proteinase, pilin precursor
-
-
-
-
PulO prepilin peptidase
-
-
-
-
TFPP
-
-
-
-
type 4 prepilin peptidase
-
-
-
-
type IV prepilin peptidase
-
-
VcpD
-
-
-
-
additional information
-
the enzyme belongs to the A24 peptidase family
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
Asp17 and Asp78 are the catalytic residues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
202833-59-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prepilin PilA + H2O
?
show the reaction diagram
-
cosynthesis of PilD with its full-length substrate, PilA, leads to complete cleavage of the substrate signal peptides
-
?
pilin type-IV precursor + H2O
pilin type-IV
show the reaction diagram
-
-
-
-
?
PilS2 + H2O
?
show the reaction diagram
-
precursor of the major pilus subunit
-
-
?
prepilin type IV + H2O
pilin type IV + prepilin type IV leader peptide
show the reaction diagram
type IV Flp1 prepilin + H2O
type IV Flp1 pilin + type IV Flp1 prepilin leader peptide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
prepilin PilA + H2O
?
show the reaction diagram
-
cosynthesis of PilD with its full-length substrate, PilA, leads to complete cleavage of the substrate signal peptides
-
?
prepilin type IV + H2O
pilin type IV + prepilin type IV leader peptide
show the reaction diagram
-
prepilin maturation is required for extracellular protein secretion and DNA uptake, overview
-
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
p-chloromercuriphenylsulfonate
-
-
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
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
integral protein
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the cytoplasmic domain contains two pairs of conserved Cys residues important for activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D17A
-
site-directed mutagenesis, inactive mutant
D17A/D78A
-
site-directed mutagenesis, inactive mutant
D78A
-
site-directed mutagenesis, inactive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from membrane by detergent solubilization and immunoaffinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fppA, DNA and amino acid sequence determination and analysis, expression of wild-type and mutants in strain PAO1, method optimization
-
pilD mutants with excretion defect, expression in Escherichia coli DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lory, S.; Strom, M.S.
Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa
Gene
192
117-121
1997
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; Tommassen, J.
Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase
Mol. Microbiol.
6
1121-1131
1992
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Nunn, D.N.; Lory, S.
Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase
Proc. Natl. Acad. Sci. USA
89
47-51
1992
Pseudomonas aeruginosa, Pseudomonas aeruginosa mutant
Manually annotated by BRENDA team
Dupuy, B.; Deghmane, A.; Taha, M.
Type IV prepilin peptidase
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
204-208
2004
Bacillus subtilis, Dickeya chrysanthemi, Escherichia coli, Klebsiella pneumoniae, Legionella pneumoniae, Neisseria gonorrhoeae, Pseudomonas aeruginosa, Vibrio cholerae serotype O1, Vibrio vulnificus, Xanthomonas campestris
-
Manually annotated by BRENDA team
de Bentzmann, S.; Aurouze, M.; Ball, G.; Filloux, A.
FppA, a novel Pseudomonas aeruginosa prepilin peptidase involved in assembly of type IVb pili
J. Bacteriol.
188
4851-4860
2006
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Ng, S.Y.; Chaban, B.; Jarrell, K.F.
Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications
J. Mol. Microbiol. Biotechnol.
11
167-191
2006
Escherichia coli, Methanococcus maripaludis, Methanococcus voltae, Pseudomonas aeruginosa, Saccharolobus solfataricus
Manually annotated by BRENDA team
Bernard, C.S.; Bordi, C.; Termine, E.; Filloux, A.; de Bentzmann, S.
Organization and PprB-dependent control of the Pseudomonas aeruginosa tad Locus, involved in Flp pilus biology
J. Bacteriol.
191
1961-1973
2009
Pseudomonas aeruginosa (P22610), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Carter, M.Q.; Chen, J.; Lory, S.
The Pseudomonas aeruginosa pathogenicity island PAPI-1 is transferred via a novel type IV pilus
J. Bacteriol.
192
3249-3258
2010
Pseudomonas aeruginosa
Manually annotated by BRENDA team
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
Pseudomonas aeruginosa (P22610), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (P22610)
Manually annotated by BRENDA team