ProGlyProt ID BC142 Organism Information Organism Name Flavobacterium meningosepticum (Elizabethkingia meningoseptica) Domain Bacteria Classification Family: Flavobacteriaceae Order: "Flavobacteriales" Class: Flavobacteria Division or phylum: "Bacteroidetes" Taxonomic ID (NCBI) 238 Genome Sequence (s) EMBL L06331 Gene Information Gene Name endO F2 NCBI Gene ID Protein Information Protein Name Endo-β-N-acetylglucosaminidase F2 UniProtKB/SwissProt ID P36912 NCBI RefSeq EMBL-CDS AAA24923.1 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 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 PDB ID 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 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 Glycosite Sequence Logo seqlogo 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]. 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) OST Gene Name OST NCBI Gene ID OST GenBank Gene Sequence OST Protein Name OST UniProtKB/ SwissProt ID OST NCBI RefSeq OST EMBL-CDS OST UniProtKB Sequence OST EC Number (BRENDA) OST Genome Context Characterized Accessory Gene(s) PGL Additional Links CAZy Literatures 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, Additional Comments Identified 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 t Year of Identification 1995 Year of Validation 1995