ProGP452

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ProGP ID ProGP452
Validation Status Characterized
Organism Information
Organism NameCamplyobacter jejuni NCTC11168
Domain Bacteria
Classification Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 192222
Genome Sequence(s)
GenBank AL111168.1
EMBL AL111168.1
Gene Information
Gene NameporA
NCBI Gene ID 905550
GenBank Gene Sequence NC_002163.1
Protein Information
Protein NameMOMP
UniProtKB/SwissProt ID P80672
NCBI RefSeq YP_002344650.1
EMBL-CDSCAL35374.1
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 LocationCell 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 ProteinT268
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
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionAltered 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.
Technique(s) used for Glycan Identification Biotinylated labelled lectins (such as Jacalin lectin) and antibodies against glycans.
Protein Glycosylation linked (PGL) gene(s)
OST ProGT IDProGT16
Accessory Gene(s)Progt IDProGT16.1-ProGT16.10
Literature
Year of Identification2014
Year of Identification Month Wise2014.1.1
Year of Validation 2014
Reference Mahdavi J, Pirinccioglu N, Oldfield NJ, Carlsohn E, Stoof J, Aslam A, Self T, Cawthraw SA, Petrovska L, Colborne N, Sihlbom C, Borén T, Wooldridge KG, AlaAldeen DA. (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 Biol., 4:130202. [PMID: 24451549]
AuthorMahdavi J, Pirinccioglu N, Oldfield NJ, Carlsohn E, Stoof J, Aslam A, Self T, Cawthraw SA, Petrovska L, Colborne N, Sihlbom C, Borén T, Wooldridge KG, AlaAldeen DA
Research GroupSchool of Life Sciences, University of Nottingham, Nottingham NG7 2RD, UK
Corresponding Author AlaAldeen DA
ContactSchool of Life Sciences, University of Nottingham, Nottingham NG7 2RD, UK