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Information on EC 3.6.1.15 - nucleoside-triphosphate phosphatase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC3.6.1.15
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EC Tree
IUBMB Comments
The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin .
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
ntpase, ntpdase, nucleoside triphosphatase, ntpdase1, ntpdase2, nsp13, kidins220, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate hydrolase, pvx cp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GP086L protein
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M86L protein
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MC100R
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-
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NTPase
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nucleoside 5-triphosphatase
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nucleoside triphosphate phosphohydrolase
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nucleoside-5-triphosphate phosphohydrolase
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phosphatase, nucleoside tri-
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T4P motor protein
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type IV pilus motor protein
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additional information
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PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
unspecific diphosphate phosphohydrolase
The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9075-51-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
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recombinant His-tagged PilB, PilT, and PilU show ATPase activity in vitro with requirement for three invariant acidic residues in the Asp Box motif, and for two invariant His residues in the His Box motif to varying extents, overview
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?
NTP + H2O
NDP + phosphate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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activity of mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes pilB, pilT and pilU
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A069PWZ3_PSEAI
120
0
12518
TrEMBL
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A0A0A8RK07_PSEAI
181
0
19908
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the type IV pilus motor proteins contain conserved residues in the Walker A, Walker B, and Asp Box and His Box motifs characteristic of secretion NTPases, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D160N
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site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
E159Q
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site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
E163Q
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site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
E204Q
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site-directed mutagenesis, mutation of the Walker B motif residue in PilT
G135S
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site-directed mutagenesis, mutation of the Walker A motif residue in PilT
H222A
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site-directed mutagenesis, mutation of the His Box motif residue in PilT
H229A
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site-directed mutagenesis, mutation of the His Box motif residue in PilT
additional information
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mutation of conserved Walker A or Walker B residues in any of the three ATPases abrogates twitching motility, and for the Walker A mutant of PilT causes loss of polar localization, construction of diverse mutants of the type IV pilus motor proteins, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain Bl21 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes pilB, pilT and pilU, DNA and amino acid sequence determination and anaylsis, expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Bl21
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chiang, P.; Sampaleanu, L.M.; Ayers, M.; Pahuta, M.; Howell, P.L.; Burrows, L.L.
Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU
Microbiology
154
114-126
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAK
Manually annotated by BRENDA team