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
Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W.
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XcpT-W are PilD-processed, N-methylated prepilin-like proteins located in the inner membrane before and after leader removal.
"the precursor forms of XcpT-W are located predominantly in the bacterial inner membrane, and their localization is not altered after PilD-mediated removal of the leader sequence"
GSP-dependent protein secretion in gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa.
Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase.
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Four linked prepilin-like genes (pddA-D, later xcpT-W) are required for protein excretion.
"Site-specific mutations within these genes have shown that they are required for protein excretion"
Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion.
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His-tagged XcpT forms stoichiometric complexes with XcpV, among other pseudopilins.
"an oligohistidine-tagged XcpT was shown to form stoichiometric complexes with PilA, and with XcpT, U, V and W"
The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus.
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XcpV nucleates the tip complex, binding XcpX and XcpW at different sites.
"We propose a model in which XcpV(I) is the nucleator that first binds XcpX(K) and XcpW(J) at different sites"
Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.
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XcpV and XcpW form the core of the pseudopilus tip; the xcpV mutant has the lowest LasB secretion and is complemented.
"Taken together, these results fully support that XcpV and -W form a core complex indispensable to T2SS functions."
UniProt entry Q00516 (GSPI_PSEAE)
PAINT node leaf composition for the XcpS, XcpW and XcpV seed nodes