ProGP509 (Ccop)
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| ProGP ID | ProGP509 (Ccop) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Neisseria meningitidis C311 and MC58 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Betaproteobacteria Orders : Neisseriales Family : Neisseriaceae Genus : Neisseria Species : meningitidis Strain : C311 and MC58 |
| Taxonomic ID (NCBI) | 491 |
| Genome Information | |
| GenBank | AE002098.2 |
| EMBL | AE002098 |
| Organism Additional Information | Neisseria meningitidis (Gram-negative bacterium) is the causative agent of cerebrospinal meningitis. Sometimes, it crosses the epithelium using its pili to enter the bloodstream. After rapid proliferation, this leads to septicemia. It also crosses the blood-brain barrier to proliferate in the brain. |
| Gene Information | |
| Gene Name | ccop (NMB_1723) or fixP |
| Protein Information | |
| Protein Name | Ccop |
| UniProtKB/SwissProt ID | Q9JY60 |
| NCBI RefSeq | WP_002244268.1 |
| EMBL-CDS | AAF42068.2 |
| UniProtKB Sequence | >tr|Q9JY60|Q9JY60_NEIMB Cytochrome c oxidase, subunit III OS=Neisseria meningitidis serogroup B (strain MC58) GN=fixP PE=4 SV=1 MNTTSQFTSNFWNIYIAVIVLLSFIALAWLLLSQNVVKRPKKGEEVQTTGHEWDGIAEYD NPLPRWWFWLCVLTWLFGIGYLVMYPGVGDYKGLLKWTSHNQYEKEVKKADEQYGKLYAK FADMPIEKVAKDPQAKQIAQNLFNTYCIQCHGSDAKGSKGFPNLTDSDWLWGGDPDKIHE TIEKGRVATMPAWGPALGEEGVKDVAHYVMSLSKPEGQYDEERAARGQALFSGPPANCFT CHGDKGQGIQGLGPNLTDDVWLWGGTQKSIIETITNGRSSQMPAWGHFLDKDKLHIMTAY VWGLSDKDGKAPVKKAEPAPTPAPAAEPAASAPAEAAQAVSEAKPAAAEPKAEEKAAPAA KADGK |
| Sequence length | 365 AA |
| Subcellular Location | Membrane |
| Function | Cytochrome c oxidase, subunit III |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser/Thr) linked |
| Technique(s) used for Glycosylation Detection | Mass Spectrometry |
| Literature | |
| Year of Identification | 2015 |
| Year of Identification Month Wise | 2015.5.1 |
| Reference | Schulz, B.L., Jen, F.E., Power, P.M., Jones, C.E., Fox, K.L., Ku, S.C., Blanchfield, J.T. and Jennings, M.P., 2013. Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates. PloS one, 8(5), p.e62768. |
| Corresponding Author | Mario F Feldman |
| Contact | School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. |