ProGP305 (Laz)
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ProGP ID | ProGP305 (Laz) |
Validation Status | Uncharacterized |
Organism Information | |
Organism Name | Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) |
Domain | Bacteria |
Classification | Phylum : Proteobacteria Class : Betaproteobacteria Orders : Neisseriales Family : Neisseriaceae Genus : Neisseria Species : gonorrhoeae Strain : strain ATCC 700825 / FA 1090 |
Taxonomic ID (NCBI) | 242231 |
Genome Information | |
GenBank | AE004969.1 |
EMBL | AE004969 |
Organism Additional Information | Neisseria gonorrhoeae is the etiologic agent of the human disease gonorrhoea. It is equipped with a variety of adherence factors that help it in the colonization of diverse microenvironments in the human host. The property of phase and antigenic variation displayed by its type IV pilin enables it to avoid immune system thereby initiating the disease. |
Gene Information | |
Gene Name | NGO0994 |
NCBI Gene ID | 3281780 |
GenBank Gene Sequence | NC_002946.2 |
Protein Information | |
Protein Name | Laz |
UniProtKB/SwissProt ID | Q5F809 |
NCBI RefSeq | WP_003688275.1 |
EMBL-CDS | AAW89678.1 |
UniProtKB Sequence | >tr|Q5F809|Q5F809_NEIG1 Lipid modified azurin protein OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) GN=NGO0994 PE=4 SV=1 MKAYLALISAAVIGLAACSQEPAAPAAEATPAGEAPASEAPAAEAAPADAAEAPAAGNCA ATVESNDNMQFNTKDIQVSKACKEFTITLKHTGTQPKASMGHNLVIAKAEDMDGVFKDGV GAADTDYVKPDDARVVAHTKLIGGGEESSLTLDPAKLADGDYKFACTFPGHGALMNGKVT LVD |
Sequence length | 183 AA |
Subcellular Location | Periplasm |
Function | Lipid-modified azurin Cu binding resistance to oxidative stress. |
Glycosylation Status | |
Technique(s) used for Glycosylation Detection | Immunoblotting using anti glycan antibodies |
Literature | |
Year of Identification | 2009 |
Year of Identification Month Wise | 2009.3 |
Reference | Vik, Å., Aas, F.E., Anonsen, J.H., Bilsborough, S., Schneider, A., Egge-Jacobsen, W. and Koomey, M., 2009. Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae. Proceedings of the National Academy of Sciences, 106(11), pp.4447-4452. |
Corresponding Author | Wolfgang Egge-Jacobsen Michael Koomey |
Contact | a.Department of Molecular Biosciences and b.Center for Molecular Biology and Neuroscience, University of Oslo, Oslo 0316, Norway |