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ProGlyProt ID
BC142
Organism Information
Organism Name
Elizabethkingia meningoseptica (Flavobacterium meningosepticum)
Domain
Bacteria
Classification
Family: Flavobacteriaceae
Order: "Flavobacteriales"
Class: Flavobacteria
Division or phylum: "Bacteroidetes"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
EMBL
 
 
Gene Information
Gene Name
endO F2
 
 
Protein Information
Protein Name
Endo-β-N-acetylglucosaminidase F2
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
Sequence length
335 AA
Subcellular Location
Periplasm (secreted)
Function
Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Complex biantennary glycans are the preferred substrates. EC= 3.2.1.96.
 
 
Protein Structure
Homology Model
Homology Model File
 
 
Glycosylation Status
Glycosylation Type
O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein
(Signal peptide: 1-45) S73, S89, S143
Experimentally Validated Glycosite(s ) in Mature Protein
S28, S44, S98
Glycosite(s) Annotated Protein Sequence
>sp|P36912|EBA2_FLAME Endo-beta-N-acetylglucosaminidase F2 OS=Flavobacterium men
ingosepticum GN=endOF2 PE=1 SV=1 MKTANFSFALCLSVVIMLFIKCTRSEQDLSVTKDAIAQKSGV
TVSAVNLSNLIAYKNSDH QISAGYYRTWRDS*(73)ATASGNLPSMRWLPDS*(89)LDMVMVFPDTPPE
NAYWNTLKTNYVPYLHK RGTKVIITLGDLNSATTTGGQDS*(143)IGYSSWAKGIYDKWVGEYNLDGIDID
IESSPSGATLT KFVAATKALSKYFGPKSGTGKTFVYDTNQNPTNFFIQTAPRYNYVFLQAYGRSTTNLTTV S
GLYAPYISMKQFLPGFSFYEENGYPGNYWNDVRYPQNGTGRAYDYARWQPATGKKGGVF SYAIERDAPLTSSND
NTLRAPNFRVTKDLIKIMNP
Sequence Around Glycosites (21 AA)
SAGYYRTWRDSATASGNLPSM
NLPSMRWLPDSLDMVMVFPDY
NSATTTGGQDSIGYSSWAKGI
Glycosite Sequence Logo
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection
Mass shift detected on SDS-polyacrylamide gel and phenol-sulfuric acid assay
Technique(s) used for Glycosylated Residue(s) Detection
Edman degradation and collision activated dissociation (CAD) mass spectrometry
Protein Glycosylation- Implication
Glycosylation may contribute towards protein stability
 
 
Glycan Information
Glycan Annotation
Linkage: Man- Ser.
Branched acidic, heptasaccharide (1244 Da) containing 3 different uronyl analogs (uronic acid derivatives), a methylated Rham and Man, a Glc, and a reducing terminal Man. Only pyranose ring forms were detected [(2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU-4[(2-OMe)Rham1-2]Man].
BCSDB ID
Technique(s) used for Glycan Identification
ESI-MS (electrospray ionization mass spectrometry), CID (collision-induced dissociation), and a combination of isotopic labeling, composition and methylation analysis.
 
 
Literature
Reference(s)
1) Plummer, T.H., Jr., Tarentino, A.L. and Hauer, C.R. (1995) Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites. J Biol Chem, 270, 13192-13196. [PubMed: 7768916]
2) Reinhold, B.B., Hauer, C.R., Plummer, T.H. and Reinhold, V.N. (1995) Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum. J Biol Chem, 270, 13197-13203. [PubMed: 7768917]
3) Tarentino, A.L., Quinones, G., Changchien, L.M. and Plummer, T.H., Jr. (1993) Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression. J Biol Chem, 268, 9702-9708. [PubMed: 8486657]
Additional Comments
Glycosylation sequon features: Consensus sequon observed Asp-Ser (DS) or Asp-Thr-Thr (DTT), at turns.
DT alone may not serve as a sequon. Interestingly, the experimentally examined other five nonglycosylated DT sequons were followed by N, D and Q.
Post translational modification of 4-kDa was detected by MS in 1993 (Ref. no. 3). This PTM was seen on S28 and S44 by Edman degradation. The protein migrated slowly on SDS-PAGE (compared to its theoretical weight) and was found to be heterogeneous by MS.
Year of Identification
1995
Year of Validation
1995
 
 
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