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

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:1588814

Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase.

XcpA/PilD processes the Xcp pseudopilins in vivo.

"suggesting that XcpA is involved in the processing of these Xcp proteins. This could indeed be demonstrated in vivo."

PMID:1671384

Multiple roles of the pilus biogenesis protein pilD: involvement of pilD in excretion of enzymes from Pseudomonas aeruginosa.

pilD mutants accumulate secreted exoproteins in the periplasm.

"pilD mutants accumulate these proteins in the periplasmic space"

PMID:1898929

Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO.

XcpA (PilD) localises to the cytoplasmic membrane.

"This is consistent with a localization in the cytoplasmic membrane in P. aeruginosa"

PMID:10625704

The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases.

Type 4 prepilin peptidases are aspartic proteases; catalytic Asp pairs identified in V. cholerae TcpJ and VcpD are conserved family-wide.

"Corresponding aspartate residues are completely conserved throughout this extensive peptidase family."

PMID:23255525

Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD.

Purified PilD cleaves the PilA signal peptide and performs SAM-dependent methylation of mature pilin; zinc is needed for methylation only.

"Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage."

PMID:8096341

A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family.

PilD cleaves prepilin leader peptides and N-methylates mature pilin using SAM.

"PilD is a bifunctional enzyme with proteolytic and methylation activities carried out within two distinct active sites"

PMID:8331069

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

PilD cleaves and methylates XcpT-W in the inner membrane.

"This bifunctional enzyme, acting in the inner membrane, cleaves the leader peptides from precursors of pilins and XcpT-W"

PMID:8340405

Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa.

Four conserved cytoplasmic Cys are required for full peptidase and methylase activity.

"the 4 conserved cysteines in the cytoplasmic domain are required for full peptidase activity in vivo and for complete peptidase and methyltransferase activities in vitro"

PMID:9466269

Type II protein secretion by Pseudomonas aeruginosa: genetic suppression of a conditional mutation in the pilin-like component XcpT by the cytoplasmic component XcpR.

PMID:9668097

Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo.

Methylation-deficient PilD variants still support assembly of functional pili.

"Absence of N-methyltransferase activity did not appear to interfere with the ability of P. aeruginosa to assemble functional pili."

file:PSEAE/pilD/pilD-uniprot.txt

UniProt entry P22610 (LEP4_PSEAE)