ProGP505 (Laz (lipid-modified azurin))
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| ProGP ID | ProGP505 (Laz (lipid-modified azurin)) |
| 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 | laz (NMB_1533) |
| Protein Information | |
| Protein Name | Laz (lipid-modified azurin) |
| UniProtKB/SwissProt ID | P57026 |
| NCBI RefSeq | WP_002225055.1 |
| EMBL-CDS | AAF41888.2 |
| UniProtKB Sequence | >sp|P57026|H8_NEIMB Outer membrane protein H.8 OS=Neisseria meningitidis serogroup B (strain MC58) GN=NMB1533 PE=3 SV=1 MKAYLALISAAVIGLAACSQEPAAPAAEATPAAEAPASEAPAAEAAPADAAEAPAAGNCA ATVESNDNMQFNTKDIQVSKACKEFTITLKHTGTQPKASMGHNLVIAKAEDMDGVFKDGV GAADTDYVKPDDARVVAHTKLIGGGEEASLTLDPAKLADGEYKFACTFPGHGALMNGKVT LVD |
| Sequence length | 183 AA |
| Subcellular Location | Outer membrane |
| Function | The Laz protein is very similar to azurin, a periplasmic protein, which belongs to the copper-containing proteins in the cupredoxin superfamily. Cupredoxins are usually involved in electron transport and energy metabolism. |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser/Thr) linked |
| Technique(s) used for Glycosylation Detection | Mass Spectrometry |
| Protein Glycosylation linked (PGL) gene(s) | |
| Additional Comment | Laz is minimally glycosylated. Due to this reason, its glycosylated forms were detected by MS analysis after glycan-specific enrichment and were not detectable by western blot. |
| 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 | Michael P Jennings |
| Contact | School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. |