ProGP448 (MOMP)
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| ProGP ID | ProGP448 (MOMP) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Camplyobacter jejuni NCTC11168 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Epsilonproteobacteria Orders : Campylobacterales Family : Campylobacteraceae Genus : Campylobacter Species : jejuni Subspecies : jejuni Strain : NCTC11168 |
| Taxonomic ID (NCBI) | 192222 |
| Genome Information | |
| GenBank | AL111168.1 |
| EMBL | AL111168.1 |
| Organism Additional Information | Campylobacter jejuni is a microaerophilic, Gram-negative, human pathogen that is the major cause of bacterial food-borne diarrhoea (gastroenteritis). It is most frequently responsible for a form of post-infection neuromuscular paralysis known as Guillain Barre' syndrome. It also leads to an immunoproliferative small intestine disease that is a rare malignant lymphoma of the intestine. Motility is essential for pathogenicity. |
| Gene Information | |
| Gene Name | porA |
| NCBI Gene ID | 905550 |
| GenBank Gene Sequence | NC_002163.1 |
| Protein Information | |
| Protein Name | MOMP |
| UniProtKB/SwissProt ID | P80672 |
| NCBI RefSeq | YP_002344650.1 |
| EMBL-CDS | CAL35374.1 |
| UniProtKB Sequence | >sp|P80672|PORA_CAMJE Major outer membrane protein OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=porA PE=1 SV=3 MKLVKLSLVAALAAGAFSAANATPLEEAIKDVDVSGVLRYRYDTGNFDKNFVNNSNLNNS KQDHKYRAQVNFSAAIADNFKAFVQFDYNAADGGYGANGIKNDQKGLFVRQLYLTYTNED VATSVIAGKQQLNLIWTDNAIDGLVGTGVKVVNNSIDGLTLAAFAVDSFMAAEQGADLLE HSNISTTSNQAPFKVDSVGNLYGAAAVGSYDLAGGQFNPQLWLAYWDQVAFFYAVDAAYS TTIFDGINWTLEGAYLGNSLDSELDDKTHANGNLFALKGSIEVNGWDASLGGLYYGDKEK ASTVVIEDQGNLGSLLAGEEIFYTTGSRLNGDTGRNIFGYVTGGYTFNETVRVGADFVYG GTKTEAANHLGGGKKLEAVARVDYKYSPKLNFSAFYSYVNLDQGVNTNESADHSTVRLQA LYKF |
| Sequence length | 424 AA |
| Subcellular Location | Cell outer membrane |
| Function | Major outer membrane protein (45 kDa MOMP) is an essential multi-functional porin. It is a BgAg (human histo-blood group , Assembles to form a functional porin. May be one of the structures responsible for adhesion to intestinal cells.antigen)-binding adhesin, as is the flagellin. |
| Glycosylation Status | |
| Glycosylation Type | O- (Thr) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | T268 |
| Glycosite(s) Annotated Protein Sequence | >sp|P80672|PORA_CAMJE Major outer membrane protein OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=porA PE=1 SV=3 MKLVKLSLVAALAAGAFSAANATPLEEAIKDVDVSGVLRYRYDTGNFDKNFVNNSNLNNS KQDHKYRAQVNFSAAIADNFKAFVQFDYNAADGGYGANGIKNDQKGLFVRQLYLTYTNED VATSVIAGKQQLNLIWTDNAIDGLVGTGVKVVNNSIDGLTLAAFAVDSFMAAEQGADLLE HSNISTTSNQAPFKVDSVGNLYGAAAVGSYDLAGGQFNPQLWLAYWDQVAFFYAVDAAYS TTIFDGINWTLEGAYLGNSLDSELDDKT*(268)HANGNLFALKGSIEVNGWDASLGGLYYGDKEK ASTVVIEDQGNLGSLLAGEEIFYTTGSRLNGDTGRNIFGYVTGGYTFNETVRVGADFVYG GTKTEAANHLGGGKKLEAVARVDYKYSPKLNFSAFYSYVNLDQGVNTNESADHSTVRLQA LYKF |
| Sequence Around Glycosites (21 AA) | NSLDSELDDKTHANGNLFALK |
| Technique(s) used for Glycosylation Detection | Altered mobility revealed on immunoblots |
| Technique(s) used for Glycosylated Residue(s) Detection | LC-MS/MS analysis |
| Protein Glycosylation- Implication | Through modelling, it was shown that glycosylation significantly affects the conformation of MOMP and modulates BgAg-binding capacity. The glycosylation also facilitates biofilm formation cell-cell binding and adhesion to Caco-2 cells. Role of O-glycosylation in pathogenesis was demonstrated by glycosylation-driven optimal colonization of chickens by C. jejuni. |
| Glycan Information | |
| Glycan Annotation | The glycan identified was a T-antigen, Gal(β1-3)-GalNAc(β1-4)-GalNAc(β1-4)-GalNAcα1-Thr268. |
| GlyTouCan | G77932VT |
| Technique(s) used for Glycan Identification | Biotinylated labelled lectins (such as Jacalin lectin) and antibodies against glycans. |
| Literature | |
| Year of Identification | 2014 |
| Year of Identification Month Wise | 2014.1.1 |
| Year of Validation | 2014 |
| Reference | Mahdavi, J., Pirinccioglu, N., Oldfield, N.J., Carlsohn, E., Stoof, J., Aslam, A., Self, T., Cawthraw, S.A., Petrovska, L., Colborne, N. and Sihlbom, C., 2014. A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization. Open biology, 4(1), p.130202. |
| Corresponding Author | Jafar Mahdavi Dlawer A. A. Ala’Aldeen |
| Contact | School of Life Sciences, University of Nottingham, Nottingham NG7 2RD, UK |