ProGP114 (Endo-β-N-acetylglucosaminidase F2)

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ProGP ID ProGP114 (Endo-β-N-acetylglucosaminidase F2)
Validation Status Characterized
Organism Information
Organism NameFlavobacterium meningosepticum (Elizabethkingia meningoseptica)
Domain Bacteria
Taxonomic ID (NCBI) 238
Genome Information
GenBank L06331
EMBL L06331
Gene Information
Gene NameendO F2
Protein Information
Protein NameEndo-β-N-acetylglucosaminidase F2
UniProtKB/SwissProt ID P36912
EMBL-CDSAAA24923.1
UniProtKB Sequence >sp|P36912|EBA2_FLAME Endo-beta-N-acetylglucosaminidase F2 OS=Flavobacterium meningosepticum GN=endOF2 PE=1 SV=1 MKTANFSFALCLSVVIMLFIKCTRSEQDLSVTKDAIAQKSGVTVSAVNLSNLIAYKNSDH QISAGYYRTWRDSATASGNLPSMRWLPDSLDMVMVFPDYTPPENAYWNTLKTNYVPYLHK RGTKVIITLGDLNSATTTGGQDSIGYSSWAKGIYDKWVGEYNLDGIDIDIESSPSGATLT KFVAATKALSKYFGPKSGTGKTFVYDTNQNPTNFFIQTAPRYNYVFLQAYGRSTTNLTTV SGLYAPYISMKQFLPGFSFYEENGYPGNYWNDVRYPQNGTGRAYDYARWQPATGKKGGVF SYAIERDAPLTSSNDNTLRAPNFRVTKDLIKIMNP
Sequence length 335 AA
Subcellular LocationPeriplasm (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.
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 ProteinS28, S44, S98
Glycosite(s) Annotated Protein Sequence >sp|P36912|EBA2_FLAME Endo-beta-N-acetylglucosaminidase F2 OS=Flavobacterium meningosepticum GN=endOF2 PE=1 SV=1 MKTANFSFALCLSVVIMLFIKCTRSEQDLSVTKDAIAQKSGVTVSAVNLSNLIAYKNSDH QISAGYYRTWRDS*(73)ATASGNLPSMRWLPDS*(89)LDMVMVFPDTPPENAYWNTLKTNYVPYLHK RGTKVIITLGDLNSATTTGGQDS*(143)IGYSSWAKGIYDKWVGEYNLDGIDIDIESSPSGATLT KFVAATKALSKYFGPKSGTGKTFVYDTNQNPTNFFIQTAPRYNYVFLQAYGRSTTNLTTV SGLYAPYISMKQFLPGFSFYEENGYPGNYWNDVRYPQNGTGRAYDYARWQPATGKKGGVF SYAIERDAPLTSSNDNTLRAPNFRVTKDLIKIMNP
Sequence Around Glycosites (21 AA) SAGYYRTWRDSATASGNLPSM
NLPSMRWLPDSLDMVMVFPDY
NSATTTGGQDSIGYSSWAKGI
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Technique(s) used for Glycosylation DetectionMass 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 137520
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.
Protein Glycosylation linked (PGL) gene(s)
Additional CommentIdentified 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.
Literature
Year of Identification1995
Year of Identification Month Wise1995.06.02
Year of Validation 1995
ReferencePlummer, T.H., 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∗. Journal of Biological Chemistry, 270(22), pp.13192-13196.
Corresponding Author Thomas H Plummer Jr
ContactDivision of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.
Reference 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]
Corresponding Author Vernon N Reinhold
ContactDepartment of Immunology Boston University Medical Center 80 East Concord ST Boston
ReferenceTarentino, A.L., Quinones, G., Changchien, L.M. and Plummer, T.H., 1993. Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression. Journal of Biological Chemistry, 268(13), pp.9702-9708.
Corresponding Author Thomas H Plummer Jr
A L Tarentino
ContactDivision of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.