ProGP1268 (Conserved hypothetical protein)

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ProGP ID ProGP1268 (Conserved hypothetical protein)
Validation Status Characterized
Organism Information
Organism NameHaloferax volcanii DS2
Domain Archaea
Classification Phylum : Euryarchaeota
Class : Halobacteria
Orders : Haloferacales
Family : Haloferacaceae
Genus : Haloferax
Species : volcanii
Strain : DS2
Taxonomic ID (NCBI) 2246
Genome Information
GenBank M62816
EMBL M62816
Organism Additional Information It is an easily culturable moderate halophile
Gene Information
Gene NameHVO_2167
Protein Information
Protein NameConserved hypothetical protein
UniProtKB/SwissProt ID D4GVA0
UniProtKB Sequence >tr|D4GVA0|D4GVA0_HALVD DUF4350 domain-containing protein OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=HVO_2167 PE=4 SV=1 MRLGSREVGYPHLLVAALLVAMLVGVGVGAGTSSSTYGAFNAAWDGGSGVRGVAADAGAETEVVYNTTEYDAVDPAPAGSVAFVISPERGYTDAEAARIEAFVRAGGTVVVADDFRPHGNDLLARLGASARIDRTPLRDDRHQYKSGALPVATRVAADPLTRNVTQLSLNHPATVTANESTVLVRSSNFSYLDRDDDGELDDDETLQSHPVVTRERLGAGDVVVVSDPSVFINAMLDRPDNRAFATALVSDRATVVLDFSHAEERPPLQVALRALRDSGALQLLFGVVAAGAVALVARQGRLS
Subcellular LocationSec pathway
Function signal peptidase I
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN188
Glycosite(s) Annotated Protein Sequence SSNFSYLDRDDDGELDDDETLQSHPVVTR
Technique(s) used for Glycosylation DetectionUPLC coupled via a nanospray source to a Q-Exactive HFX tandem MS
Glycan Information
Glycan Annotation Tetrasaccharide Glc-GlcA-GalA-MeGlcA
Technique(s) used for Glycan Identification UPLC coupled via a nanospray source to a Q-Exactive HFX tandem MS
Protein Glycosylation linked (PGL) gene(s)
OST ProGT IDProGT15 (AglB)
Additional CommentGlycosylation and glycosites are predicted by glycoproteomic in-silico analysis of raw experimental data available on PRIDE and jPOST.
Literature
Year of Identification2021
ReferenceSchulze, S., Pfeiffer, F., Garcia, B.A. and Pohlschroder, M., 2021. Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea. PLoS biology, 19(6), p.e3001277.
Corresponding Author Mechthild Pohlschroder
ContactDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America