| Organism Information |
| Organism Name | Pseudomonas aeruginosa 1244 |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria
Class : GammaProteobacteria
Orders : Pseudomonadales
Family : Pseudomonadaceae
Genus : Pseudomonas
Species : aeruginosa
|
| Taxonomic ID (NCBI) | 287 |
| Genome Information |
| Gene Bank | NC_002516.2 |
| Gene Information |
| Gene Name | pilO |
| NCBI Gene ID | 880985 |
| Protein information |
| Protein Name | PilO |
| UniProtKB/ SwissProt ID | A0A1U9XPN7 |
| NCBI Ref Seq | WP_003104917.1 |
| UniProtKB Sequence | >tr|A0A1U9XPN7|A0A1U9XPN7_PSEAI Oligosaccharyl transferase OS=Pseudomonas aeruginosa GN=pilO PE=4 SV=1
MRMWLAWERMDRVLRTILLLLISILLLSPIVYCGVSDNWHDQQRILQLVVLSGSSLLLLF
SFPLPFARRMVQVTLLVILGLGSVSAFLSANPSWAFKEWSVFAGLMLFSFNISASPEWVR
RIALWGLVVLGGFFCYQFLLSYLAAFVSGLRELNPRVLLSGFSNVRTMGQFQAMLLPLMA
ALGLYLRETGRFRLSRLVMLLLAIQWCISFALAGRGLWLGFAVAHLALCWIGPVGRRFLI
VQLSAVFVGLALYFLLMVALPTWLGIDMTLMSGMRSGLSLRDVLWRDAWGMFVAHPLLGV
GPMHFSAVPNSVGAHPHQMLLQWFAEWGGVAGLLVVGLMILGLLRGARYLREQGDSMDAG
LWLALVSVLVLAQVDGVFVMPFTQTVLALLVGIAMARWSKPVAPSPAQRWLCRGLAVVVI
VVLGRVLLLEVPGLTAAEERYLEIHGGGEAPRFWIQGWIPM
|
| EMBL CDS | AQZ26225 |
| Sequence length | 461 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Function in Native Organism | 1) PilO required for pilin glycosylation and the glycosylated pilin act as a significant virulence factor during infection. |
| Potential Application | 1) PilO has relaxed specificity and can transfer the variety of glycans on acceptor substrate, this non-specific behavior of enzyme can use to design conjugate vaccines. |
| Additional Information | 1) PilO can transfer a variety of carbohydrates (only short glycan chains) other than their endogenous glycans to acceptor proteins in E.coli. |
| Glycosyltransferase Information |
| Glycosylation Type | O- (Ser/Thr) linked |
| CAZY Family | GTNC |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | En bloc |
| Acceptor specificity Sequon_1 | Carboxy-terminal serine |
| Donor Type | UndPP-Trisaccharide |
| Donor Specificity | Lipid linked sugars |
| Accessory GT ID | ProGT1.1,ProGT1.2 |
| Glycan Information |
| Glycan transferred | Trisaccharide (alpha-5NBetaOHC(4)7NFmPse-(2-->4)Beta-Xyl-(1-->3)-Beta-FuNAc) |
| Method of Glycan Indentification | MALDI-TOF, FT ICR, and nanoESI QTOF MS |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information |
| Acceptor Substrate name | PilA |
| ProGPdb ID | ProGP230 |
| Litrature |
| Year Of Validation | 1995 |
| Reference | Castric, P., 1995. pilO, a gene required for glycosylation of Pseudomonas aeruginosa 1244 pilin. Microbiology, 141(5), pp.1247-1254.
|
| Corresponding Author | Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
|
| Reference | Faridmoayer, A., Fentabil, M.A., Mills, D.C., Klassen, J.S. and Feldman, M.F., 2007. Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation. Journal of bacteriology, 189(22), pp.8088-8098.
|
| Corresponding Author | Alberta Ingenuity Centre for Carbohydrate Science, Canada
|
| Reference | Qutyan, M., Paliotti, M. and Castric, P., 2007. PilO of Pseudomonas aeruginosa 1244: subcellular location and domain assignment. Molecular microbiology, 66(6), pp.1444-1458.
|
| Corresponding Author | Department of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
|
| Reference | Sampaleanu, L.M., Bonanno, J.B., Ayers, M., Koo, J., Tammam, S., Burley, S.K., Almo, S.C., Burrows, L.L. and Howell, P.L., 2009. Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex. Journal of molecular biology, 394(1), pp.143-159.
|
| Corresponding Author | Program in Molecular Structure and Function, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, Canada M5G 1X8
|
| Reference | Qutyan, M., Henkel, M., Horzempa, J., Quinn, M. and Castric, P., 2010. Glycosylation of pilin and nonpilin protein constructs by Pseudomonas aeruginosa 1244. Journal of bacteriology, 192(22), pp.5972-5981.
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| Corresponding Author | Department of Biological Sciences, Duquesne University, Pittsburgh, PA 15282, USA.
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