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 |