ProGP77 (Major outer membrane protein (MOMP, 40 kD))
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| ProGP ID | ProGP77 (Major outer membrane protein (MOMP, 40 kD)) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Chlamydia trachomatis serovar L2 (strain 434/Bu) |
| Domain | Bacteria |
| Classification | Phylum : Chlamydiae Class : Chlamydiia Orders : Chlamydiales Family : Chlamydiaceae Genus : Chlamydia Species : trachomatis Strain : 434/Bu |
| Taxonomic ID (NCBI) | 471472 |
| Genome Information | |
| GenBank | AM884176.1 |
| EMBL | AM884176 |
| Gene Information | |
| Gene Name | ompA (CTL0050) |
| NCBI Gene ID | 5858320 |
| GenBank Gene Sequence | NC_010287.1 |
| Protein Information | |
| Protein Name | Major outer membrane protein (MOMP, 40 kDa) |
| UniProtKB/SwissProt ID | P06597 |
| NCBI RefSeq | WP_009873292.1 |
| EMBL-CDS | CAP03494.1 |
| UniProtKB Sequence | >sp|P06597|MOMP_CHLT2 Major outer membrane porin OS=Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) GN=ompA PE=1 SV=1 MKKLLKSVLVFAALSSASSLQALPVGNPAEPSLMIDGILWEGFGGDPCDPCTTWCDAISM RMGYYGDFVFDRVLQTDVNKEFQMGAKPTTATGNAAAPSTCTARENPAYGRHMQDAEMFT NAAYMALNIWDRFDVFCTLGATSGYLKGNSASFNLVGLFGDNENHATVSDSKLVPNMSLD QSVVELYTDTTFAWSAGARAALWECGCATLGASFQYAQSKPKVEELNVLCNAAEFTINKP KGYVGQEFPLDLKAGTDGVTGTKDASIDYHEWQASLALSYRLNMFTPYIGVKWSRASFDA DTIRIAQPKSATTVFDVTTLNPTIAGAGDVKASAEGQLGDTMQIVSLQLNKMKSRKSCGI AVGTTIVDADKYAVTVETRLIDERAAHVNAQFRF |
| Sequence length | 394 AA |
| Subcellular Location | Membrane associated |
| Function | The MOMP (40 kDa protein) is the principal structural protein of the EB (infectious elementary body). Through disulfide-mediated interactions, the MOMP provides the structural integrity to the extracellular infectious form and performs a porin-like function when Chlamydiae are intracellular and metabolically active. The serological specificity of the organism resides in MOMP, and antibodies raised against MOMP neutralize infectivity of Chlamydia. |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Technique(s) used for Glycosylation Detection | Change in SDS-PAGE mobility after periodate oxidation, polysaccharide staining with p-phenylenediamine, rapid migration on SDS-PAGE after PNGaseF treatment, lectin binding (ConA, WGA, DBA), and autoradiography after metabolic labeling with [3H] glucosamine. |
| Glycan Information | |
| Glycan Annotation | Linkage: β-GlcNAc-N-Asn. The major fractions consisted of “high mannose type” oligosaccharides containing 8–9 mannose residues. Bi- and tri-antennary “complex type” oligosaccharides having terminal galactose were detected as minor components. These oligosaccharides were N-linked and contained no sialic acid. A specific high-mannose type oligosaccharide linked to the MOMP of C. trachomatis mediates attachment and infectivity of the organism to HeLa cells. The lectin-binding properties of MOMP and its susceptibility to glycosidase indicate that MOMP glycoprotein contains α-Man and β-GlcNAc at the terminus. |
| Literature | |
| Year of Identification | 1991 |
| Year of Identification Month Wise | 1991.06 |
| Reference | Kuo, C.C., Takahashi, N., Swanson, A.F., Ozeki, Y. and Hakomori, S.I., 1996. An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells. The Journal of clinical investigation, 98(12), pp.2813-2818. |
| Corresponding Author | C C Kuo S Hakomori |
| Contact | Department of Pathobiology, University of Washington, Seattle 98195, USA. Pacific Northwest Research Foundation, Biomembrane Division, 720Broadway, Seattle, Washington 98122 |
| Reference | Swanson, A.F. and Kuo, C.C., 1994. Binding of the glycan of the major outer membrane protein of Chlamydia trachomatis to HeLa cells. Infection and immunity, 62(1), pp.24-28. |
| Corresponding Author | C C Kuo |
| Contact | Department of Pathobiology, University of Washington, Seattle 98195, USA. |
| Reference | Swanson, A.F. and Kuo, C.C., 1991. Evidence that the major outer membrane protein of Chlamydia trachomatis is glycosylated. Infection and immunity, 59(6), pp.2120-2125. |
| Corresponding Author | C C Kuo |
| Contact | Department of Pathobiology, University of Washington, Seattle 98195, USA. |