ProGP505 (Laz (lipid-modified azurin))

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ProGP ID ProGP505 (Laz (lipid-modified azurin))
Validation Status Uncharacterized
Organism Information
Organism NameNeisseria meningitidis C311 and MC58
Domain Bacteria
Classification Family: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
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 Namelaz (NMB_1533)
Protein Information
Protein NameLaz (lipid-modified azurin)
UniProtKB/SwissProt ID P57026
NCBI RefSeq NP_274540.1
EMBL-CDSAAF41888.2
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 LocationOuter 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 DetectionMass Spectrometry
Literature
Year of Identification2015
Year of Identification Month Wise2015.5.1
ReferenceSchulz BL, Jen FE, Power PM, Jones CE, Fox KL, Ku SC, Blanchfield JT, Jennings MP. (2013)Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates. PLoS One, 8(5): e62768. [PubMed: 23658772]
AuthorBenjamin L. Schulz, Freda E. C. Jen, Peter M. Power, Christopher E. Jones, Kate L. Fox, Shan C. Ku, Joanne T. Blanchfield, and Michael P. Jennings
Research GroupSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
Corresponding Author Michael P. Jennings
ContactSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.