ProGP497

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ProGP ID ProGP497
Validation Status Characterized
Organism Information
Organism NameNeisseria elongata subsp. glycolytica
Domain Bacteria
Classification Family: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 546263
Genome Sequence(s)
EMBL ADBF01000023 
Gene Information
Gene NamecycC (NEIELOOT_00905)
Protein Information
Protein NameCN
UniProtKB/SwissProt ID D4DPB8
EMBL-CDSEFE50226.1.
UniProtKB Sequence >tr|D4DPB8|D4DPB8_NEIEG Uncharacterized protein OS=Neisseria elongata subsp. glycolytica ATCC 29315 GN=NEIELOOT_00905 PE=4 SV=1 MNKLLIAAMMMAALTACSQEAKQETKEAAQAIASDVKNNTASAVDAAASSVQEAASKVAD TAEKAASEVKEAVAPEAKPAEKTEAPAAKVDGKAVYEATCKACHSGTIPGTPGVGKKTSG NHVSNKVKKPCTNTRLKASKVCLPKAVTKV
Sequence length 150 AA
Function A c-type monoheme cytochrome
Glycosylation Status
Glycosylation Type O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS34, S42 and S49
Glycosite(s) Annotated Protein Sequence >tr|D4DPB8|D4DPB8_NEIEG Uncharacterized protein OS=Neisseria elongata subsp. glycolytica ATCC 29315 GN=NEIELOOT_00905 PE=4 SV=1 MNKLLIAAMMMAALTACSQEAKQETKEAAQAIAS*(32)DVKNNTAS*(42)AVDAAAS*(49)SVQEAASKVAD TAEKAASEVKEAVAPEAKPAEKTEAPAAKVDGKAVYEATCKACHSGTIPGTPGVGKKTSG NHVSNKVKKPCTNTRLKASKVCLPKAVTKV
Sequence Around Glycosites (21 AA) ETKEAAQAIASDVKNNTASAV
IASDVKNNTASAVDAAASSVQ
NTASAVDAAASSVQEAASKVA
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionDifference in mobility on immunoblots
Technique(s) used for Glycosylated Residue(s) Detection ETD fragmentation
Glycan Information
Glycan Annotation A tetrasaccharide glycoform consisting of di-N-acetylbacillosamine-glucose-di-N-acetyl hexuronic acid-N-acetylhexosamine (diNAcBac-Glc-diNAcHexA-HexNAc).
Technique(s) used for Glycan Identification Mass spectrometry
Literature
Year of Identification2014
Year of Identification Month Wise2014.6.1
Year of Validation 2016
ReferenceAas FE, Li X, Edwards J, Hongrø Solbakken M, Deeudom M, Vik Å, Moir J, Koomey M, Aspholm M. (2014) Cytochrome c-based domain modularity governs genus-level diversification of electron transfer to dissimilatory nitrite reduction. Environ Microbiol., 17(6):2114-32. [PMID: 25330335]
AuthorAas FE1, Li X2, Edwards J2, Hongrø Solbakken M1,3, Deeudom M2,4, Vik Å1, Moir J2, Koomey M1,3, Aspholm M1.
Research Group1 Department of Biosciences, University of Oslo, Oslo, N-0316, Norway. 2 Department of Biology, University of York, York, YO10 5DD, UK. 3 Centre for Ecological and Evolutionary Synthesis, University of Oslo, Oslo, N-0316, Norway. 4 Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai, 50200, Thailand.
Corresponding Author Aspholm M
ContactDepartment of Biosciences, University of Oslo, Oslo, N-0316, Norway
ReferenceAnonsen JH, Vik Å, Børud B, Viburiene R, Aas FE, Kidd SW, Aspholm M, Koomey M (2016) Characterization of a Unique Tetrasaccharide and Distinct Glycoproteome in the O-Linked Protein Glycosylation System of Neisseria elongata subsp. glycolytica. J Bacteriol., 198(2):256-67. [PMID: 26483525
AuthorAnonsen JH, Vik Å, Børud B, Viburiene R, Aas FE, Kidd SW, Aspholm M, Koomey M
Research GroupDepartment of Biosciences, University of Oslo, Oslo, Norway
Corresponding Author Koomey M
ContactDepartment of Biosciences, University of Oslo, Oslo, Norway