Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Disparate subcellular localization patterns of Pseudomonas aeruginosa Type IV pilus ATPases involved in twitching motility.
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Functional YFP-PilU localizes to the piliated pole; the N terminus determines the localization pattern.
"PilB and PilT fusions localized to both poles, while PilU fusions localized only to the piliated pole."
Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU.
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Purified P. aeruginosa PilU has ATPase activity in vitro; Walker A/B and key Asp/His box residues are needed for twitching. No nuclease activity is reported.
"Assay of purified 6xHis-tagged PilB, PilT and PilU from P. aeruginosa showed that all three proteins have ATPase activities in vitro."
Characterization of a gene, pilU, required for twitching motility but not phage sensitivity in Pseudomonas aeruginosa.
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pilU, downstream of pilT, is needed for twitching motility; pilU mutants are hyperfimbriate but, unlike pilT mutants, stay sensitive to phage PO4.
"in contrast to pilT mutants, the pilU mutants had not also acquired resistance to infection by bacteriophage PO4"
The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase.
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PilU is a bona fide retraction ATPase that works only together with PilT, in V. cholerae and in P. aeruginosa.
"In addition to demonstrating that PilU can function as a bona fide retraction ATPase, we go on to make the surprising discovery that PilU functions exclusively in a PilT-dependent manner"
Separation of Pseudomonas aeruginosa type IV pilus-dependent twitching motility and surface-sensing responses.
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Crystal structure shows PilU as a hexameric motor ATPase; pilU mutants have high cAMP, and some PilA/PilY1 alleles restore twitching without PilU.
"Together, these findings establish PilU as a co-evolved motor ATPase, likely leveraging its unique C-terminal features for distinct functional roles."
Pseudomonas aeruginosa orchestrates twitching motility by sequential control of type IV pili movements.
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PilT alone powers retraction in free solution; PilU may improve retraction in high-friction environments.
"we found that the retraction motor PilT was sufficient to generate tension and power motility in free solution, while its partner ATPase PilU may improve retraction only in high-friction environments"
Requirement of novel competence genes pilT and pilU of Pseudomonas stutzeri for natural transformation and suppression of pilT deficiency by a hexahistidine tag on the type IV pilus protein PilAI.
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In P. stutzeri, pilU inactivation leaves twitching intact but lowers transformation, so the twitching role of PilU is not universal.
"Insertional inactivation did not affect piliation, twitching motility, or PO4 infection but reduced transformation to about 10%."
Twitching motility is essential for virulence in Dichelobacter nodosus.
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In D. nodosus, pilU mutation abolishes twitching motility.
"We showed that mutation of either the pilT or pilU gene eliminated the ability to carry out twitching motility."