ProGP77

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ProGP ID ProGP77
Validation Status Uncharacterized
Organism Information
Organism NameChlamydia 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)
GenBank AM884176.1
EMBL AM884176
Gene Information
Gene NameompA (CTL0050)
NCBI Gene ID 5858320
Protein Information
Protein NameMajor outer membrane protein (MOMP, 40 kDa)
UniProtKB/SwissProt ID P06597
NCBI RefSeq YP_001654141.1
EMBL-CDSCAP03494.1
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 LocationMembrane 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 DetectionChange 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 Identification1991
Year of Identification Month Wise1991.06
ReferenceKuo, 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]
Author Hakomori, S.
Research GroupDepartment of Pathobiology, University of Washington, Seattle 98195, USA.
Corresponding Author Kuo, C., Takahashi, N., Swanson, A.F., Ozeki, Y. Hakomori, S.
ContactDepartment of Pathobiology, University of Washington, Seattle 98195, USA.
ReferenceSwanson, 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]
AuthorSwanson, A.F. Kuo, C.C.
Research GroupDepartment of Pathobiology, University of Washington, Seattle
Corresponding Author Kuo, C.C.
ContactDepartment of Pathobiology, University of Washington, Seattle
ReferenceSwanson, A.F. and Kuo, C.C. (1991) Evidence that the major outer membrane protein of Chlamydia trachomatis is glycosylated. Infect Immun, 59, 2120-2125.
AuthorSwanson, A.F. Kuo, C.C.
Research GroupDepartment of Pathobiology, University of Washington, Seattle
Corresponding Author Kuo, C.C.
ContactDepartment of Pathobiology, University of Washington, Seattle