ProGP1255 (GATase domain protein)

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ProGP ID ProGP1255 (GATase domain 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_1988
Protein Information
Protein NameGATase domain protein
UniProtKB/SwissProt ID D4GTL7
UniProtKB Sequence >tr|D4GTL7|D4GTL7_HALVD GATase domain protein OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=HVO_1988 PE=4 SV=1 MSQRNLLGGTVVFAVALGLILVGAAVAPYAVQLGGSDSADTQNAAKQAFDADELVATPGPESGEVTMDSNAASKTVLIDVGHGNDVSESDVQPLVDALVANGHQVKYLTREDAQRNFNGSLRKADAFVVVNPEQPYTGGQLAGLRSFEDAGGRVALLGDPQSAGTTSILGLITVSVSSGTTGGDAGLTSDYGVSFGSTSLYNMHDYYLNYENVYATPEGDTALTEGVDEVVFRDAAPLSISADSVSPALVSGGETRVESIRKSGPYTVAAQSETVVAIGDADFLTPESAYEADNEVLVGNLADFLVSGDKESGAPAPATPESGAPGPGGSASGPAPGSAPTQGTTPTSA
Subcellular LocationSec pathway
Function signal peptidase I
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN118, N116
Glycosite(s) Annotated Protein Sequence DAQRNFNGSLRKAD
NFNGSLR
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