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

PMID:8331069

Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W.

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"

PMID:9818381

GSP-dependent protein secretion in gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa.

Review of the Xcp type II secretion machinery of P. aeruginosa.

PMID:1309616

Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase.

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"

PMID:9282737

Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion.

XcpW cross-links with PilA and forms heterodimers with XcpT.

"XcpW and XcpU can also be crosslinked to form dimeric complexes with PilA"

PMID:19828448

The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus.

XcpW is part of the XcpU-V-W-X tip complex and recruits XcpU.

"Then the ternary complex recruits XcpU(H) through a direct interaction with XcpW(J)"

PMID:21245534

Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa type II secretion system.

1.85 A structure of XcpW shows a type IVa pilin fold; its disordered C-terminal 31 residues are dispensable for secretion.

"Deletion of this unstructured region of XcpW(J) did not prevent type II secretion in vivo"

PMID:30346996

Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.

XcpV and XcpW form the core of the pseudopilus tip; xcpW mutants have reduced LasB secretion, restored by complementation.

"The supernatant of the xcpW mutant also had less LasB activity than the mutants of xcpU and -X"

file:PSEAE/xcpW/xcpW-uniprot.txt

UniProt entry Q00517 (GSPJ_PSEAE)

file:PSEAE/xcpV/xcpV-bioinformatics/RESULTS.md

PAINT node leaf composition for the XcpS, XcpW and XcpV seed nodes