Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
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
Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate extracellular protein secretion and pilus biogenesis in Pseudomonas aeruginosa.
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Serine substitution of the conserved Walker A glycine of XcpR abolishes exotoxin A secretion, and high-level expression of the mutant protein in wild-type bacteria causes a pleiotropic secretion defect with periplasmic accumulation of secreted enzymes.
"unable to secrete exotoxin A or assemble pili, respectively."
The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus.
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XcpR dimerises through an 85-residue N-terminal region, and that dimerisation is essential for extracellular protein secretion.
"that this dimerization is essential for extracellular protein secretion."
Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa.
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XcpR has no hydrophobic segment, yet associates with the cytoplasmic membrane in wild-type cells; the association and XcpR stability require XcpY, and membrane assembly is needed for secretion.
"In a wild-type P. aeruginosa strain, XcpR was found associated with the"
Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa.
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A His-tagged XcpZ bait co-purified XcpY, and the XcpYZ unit was isolated with XcpR and XcpS as a native XcpRSYZ complex; XcpP was not stably associated.
"XcpS to form a XcpRSYZ complex which was isolated under native conditions."
Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase.
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Sequencing of xcpR to xcpX identified XcpR as a PilB homologue with a canonical nucleotide-binding site, suggesting that ATP hydrolysis energises both secretion and pilus assembly.
"two other proteins, XcpR and XcpS, show similarity to"
GSP-dependent protein secretion in gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa.
UniProt entry Q00512 (GSPE_PSEAE)