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
Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa.
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Purified XcpQ is a stable homomultimer forming large ring-shaped structures with a central cavity of about 95 Angstroms; the C-terminal part suffices for multimerisation.
"C-terminal part of XcpQ is sufficient for the formation of the multimer."
GSP-dependent protein secretion in gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa.
Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins.
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An amino acid substitution blocks secretin assembly at a dodecameric prepore stage in PulD, and the equivalent substitution has the same effect in XcpQ.
"in the Pseudomonas aeruginosa secretin XcpQ"
Structural Basis of Type 2 Secretion System Engagement between the Inner and Outer Bacterial Membranes.
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Cryo-EM of the purified 1-MDa XcpQ complex shows a pentadecameric secretin with 15-fold symmetry in the membrane region, while the N0 and N1 domains are not ordered into that symmetry, which is proposed to allow engagement with the 6-fold inner-membrane platform.
"class averages revealed that XcpQ is a pentadecameric secretin complex"
Unraveling the Self-Assembly of the Pseudomonas aeruginosa XcpQ Secretin Periplasmic Domain Provides New Molecular Insights into Type II Secretion System Secreton Architecture and Dynamics.
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The periplasmic N0-N2 domains assemble as a hexamer of dimers, nanobody interference against the secretin reproduces the secretome of an xcpQ deletion mutant, and PAO1 delta-xcpQ is the reference strain for loss of Xcp secretion.
"the supernatant profile of the wild-type strain producing vHH04 is similar to that of an xcpQ deletion mutant"
Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries.
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XcpQ reaches the outer membrane without detectable dependence on BamA or LolB and assembles spontaneously into liposomes as multimers, unlike the PilQ and PscC secretins.
"XcpQ, but not PilQ or PscC, was shown to assemble spontaneously into liposomes as multimers."
UniProt entry P35818 (GSPD_PSEAE)