| ProGlyProt ID | BU141 | | Organism Information | | Organism Name | Chlamydia trachomatis serovar L2 (strain 434/Bu) | | Domain | Bacteria | | Classification | Family: Chlamydiaceae
Order: Chlamydiales
Class: Chlamydiae
Division or phylum: "Chlamydiae" | | Taxonomic ID (NCBI) | 471472 | | Genome Sequence (s) | | GeneBank | AM884176.1 | | EMBL | AM884176 | | Gene Information | | Gene Name | ompA (CTL0050) | | NCBI Gene ID | 5858320 | | Protein Information | | Protein Name | Major outer membrane protein (MOMP, 40 kDa) | | UniProtKB/SwissProt ID | P06597 | | NCBI RefSeq | YP_001654141.1 | | 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. | | Literatures | | Reference(s) | 1) Kuo, C., Takahashi, N., Swanson, A.F., Ozeki, Y. and Hakomori, S. (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. J Clin Invest, 98, 2813-2818. [PubMed: 8981929]
2) Swanson, A.F. and Kuo, C.C. (1994) Binding of the glycan of the major outer membrane protein of Chlamydia trachomatis to HeLa cells. Infect Immun, 62, 24-28. [PubMed: 8262634]
3) Swanson, A.F. and Kuo, C.C. (1991) Evidence that the major outer membrane protein of Chlamydia trachomatis is glycosylated. Infect Immun, 59, 2120-2125. [PubMed: 1645328] | | Year of Identification | 1991 |
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