Total Record - 1

Print this rrecord

 
ProGlyProt ID
BC144
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
endOF3
 
 
Protein Information
Protein Name
Endo-β-N-acetylglucosaminidase F3
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
Sequence length
329 AA
Subcellular Location
Periplasm (secreted)
Function
Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Hydrolyzes bi- and triantennary glycans. The presence of a core-bound fucose greatly augments endo F3 activity on biantennary and, presumably, triantennary oligosaccharides. EC= 3.2.1.96.
 
 
Protein Structure
PDB ID
 
 
Glycosylation Status
Glycosylation Type
O (Thr) linked
Experimentally Validated Glycosite(s) in Full Length Protein
(Signal peptide: 1-39) T88
Experimentally Validated Glycosite(s ) in Mature Protein
T49
Glycosite(s) Annotated Protein Sequence
>sp|P36913|EBA3_FLAME Endo-beta-N-acetylglucosaminidase F3 OS=Flavobacterium men
ingosepticum GN=endOF3 PE=1 SV=1 MKKIFFAQCSILLLMLGSCSKMTEDMTPESVNKEASVKSATA
LAGSNGVCIAYYITDGRN PTFKLKDIPDKVDMVILFGLKYWSLQDT*(88)TKLPGGTGMMGSFKSYKDLDT
QIRSLQSRGIK VLQNIDDDVSWQSSKPGGFASAAAYGDAIKSIVIDKWKLDGISLDIEHSGAKPNPIPTFP G
YAATGYNGWYSGSMAATPAFLNVISELTKYFGTTAPNNKQLQIASGIDVYAWNKIMENF RNNFNYIQLQSYGAN
VSRTQLMMNYATGTNKIPASKMVFGAYAEGGTNQANDVEVAKWTP TQGAKGGMMIYTYNSNVSYANAVRDAVKN
Sequence Around Glycosites (21 AA)
FGLKYWSLQDTTKLPGGTGMM
Technique(s) used for Glycosylation Detection
Mass shift detected on SDS-polyacrylamide gel and TFA (trifluoroacetic acid) hydrolysis of intact glycopeptide followed by HPAEC chromatography on a PA-1 column
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- Thr.
Branched, acidic, heptasaccharide (1244 Da) containing 3 different uronyl analogs, 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) Waddling, C.A., Plummer, T.H., Jr., Tarentino, A.L. and Van Roey, P. (2000) Structural basis for the substrate specificity of endo-beta-N-acetylglucosaminidase F(3). Biochemistry, 39, 7878-7885. [PubMed: 10891067]
2) 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]
3) 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]
4) 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 1.2-kDa was detected by MS in 1993 (Ref. no. 4). 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
 
 
Copyright @ 2011 IMTECH
This site is best viewed in Mozilla Firefox, Internet Explorer 6 and above at screen resolution of 1024 x 768 and above.