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PSEAE:LEP4
Contents
| Species (Taxon ID) | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228). (208964) | |
| Gene Name(s) | pilD (synonyms: xcpA) | |
| Protein Name(s) | Type 4 prepilin-like proteins leader peptide-processing enzyme
Protein PilD Protein secretion protein XCPA Leader peptidase Prepilin peptidase N-methyltransferase | |
| External Links | ||
| UniProt | P22610 | |
| EMBL | M32066 M61096 AE004091 | |
| PIR | A39131 | |
| RefSeq | NP_253218.1 WP_003112839.1 | |
| ProteinModelPortal | P22610 | |
| STRING | 208964.PA4528 | |
| MEROPS | A24.001 | |
| TCDB | 3.A.15.2.1 | |
| EnsemblBacteria | AAG07916 | |
| GeneID | 877861 | |
| KEGG | pae:PA4528 | |
| PATRIC | 19843787 | |
| PseudoCAP | PA4528 | |
| eggNOG | COG1989 | |
| HOGENOM | HOG000248584 | |
| InParanoid | P22610 | |
| KO | K02654 | |
| OMA | VFWLFKL | |
| OrthoDB | EOG6F55M8 | |
| PhylomeDB | P22610 | |
| Proteomes | UP000002438 | |
| GO | GO:0016021 GO:0005886 GO:0004190 GO:0008168 | |
| InterPro | IPR010627 IPR014032 IPR000045 | |
| Pfam | PF06750 PF01478 | |
| PRINTS | PR00864 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0016485 |
protein processing |
ECO:0000315 |
P |
supplementary figure 3: An increase in mass is observed for minor pilins FimU, PilV, PilW, PilX, and PilE when pilD is inactivated, which suggests they are processed by pilD. |
complete | |||||
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000766410 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11359 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004190 |
aspartic-type endopeptidase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000766410 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0043683 |
type IV pilus biogenesis |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0015627 |
type II protein secretion system complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009297 |
pilus assembly |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008170 |
N-methyltransferase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006480 |
N-terminal protein amino acid methylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004190 |
aspartic-type endopeptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004190 |
aspartic-type endopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0997 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0008152 |
metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0032259 |
methylation |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008168 |
methyltransferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Giltner, CL et al. (2010) Pseudomonas aeruginosa minor pilins are incorporated into type IV pili. J. Mol. Biol. 398 444-61 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Strom, MS et al. (1991) Multiple roles of the pilus biogenesis protein pilD: involvement of pilD in excretion of enzymes from Pseudomonas aeruginosa. J. Bacteriol. 173 1175-80 PubMed GONUTS page
- ↑ Bally, M et al. (1992) Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase. Mol. Microbiol. 6 1121-31 PubMed GONUTS page
- ↑ Pepe, JC & Lory, S (1998) Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo. J. Biol. Chem. 273 19120-9 PubMed GONUTS page
- ↑ 6.0 6.1 Strom, MS et al. (1993) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family. Proc. Natl. Acad. Sci. U.S.A. 90 2404-8 PubMed GONUTS page
- ↑ 7.0 7.1 Aly, KA et al. (2013) Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD. Microbiologyopen 2 94-104 PubMed GONUTS page
- ↑ Kagami, Y et al. (1998) Type II protein secretion by Pseudomonas aeruginosa: genetic suppression of a conditional mutation in the pilin-like component XcpT by the cytoplasmic component XcpR. Mol. Microbiol. 27 221-33 PubMed GONUTS page
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