EBA2_ELIME
ID EBA2_ELIME Reviewed; 335 AA.
AC P36912;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Endo-beta-N-acetylglucosaminidase F2;
DE EC=3.2.1.96;
DE AltName: Full=Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2;
DE AltName: Full=Endoglycosidase F2;
DE AltName: Full=Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2;
DE Flags: Precursor;
GN Name=endOF2;
OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8486657; DOI=10.1016/s0021-9258(18)98405-x;
RA Tarentino A.L., Quinones G., Changchien L.-M., Plummer T.H. Jr.;
RT "Multiple endoglycosidase F activities expressed by Flavobacterium
RT meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary
RT sequence, and enzyme expression.";
RL J. Biol. Chem. 268:9702-9708(1993).
RN [2]
RP GLYCOSYLATION AT SER-73; SER-89 AND SER-143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=7768916; DOI=10.1074/jbc.270.22.13192;
RA Plummer T.H. Jr., Tarentino A.L., Hauer C.R.;
RT "Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum
RT proteins. Asp-Ser and Asp-Thr-Thr consensus sites.";
RL J. Biol. Chem. 270:13192-13196(1995).
RN [3]
RP STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7768917; DOI=10.1074/jbc.270.22.13197;
RA Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N.;
RT "Detailed structural analysis of a novel, specific O-linked glycan from the
RT prokaryote Flavobacterium meningosepticum.";
RL J. Biol. Chem. 270:13197-13203(1995).
CC -!- FUNCTION: Endohydrolysis of the di-N-acetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins. Complex biantennary glycans
CC are the preferred substrates. Tri- and tetraantennary glycans are not
CC hydrolyzed, and high mannose glycans are very poor substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins containing the
CC -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue
CC remains attached to the protein, the rest of the oligosaccharide is
CC released intact.; EC=3.2.1.96;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Carbohydrates at Ser-73, Ser-89 and Ser-143 consist of (2-
CC OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
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DR EMBL; L06331; AAA24923.1; -; Genomic_DNA.
DR PIR; A46678; A46678.
DR AlphaFoldDB; P36912; -.
DR SMR; P36912; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; P36912; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..45
FT CHAIN 46..335
FT /note="Endo-beta-N-acetylglucosaminidase F2"
FT /id="PRO_0000011956"
FT DOMAIN 61..321
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 73
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7768916"
FT CARBOHYD 89
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7768916"
FT CARBOHYD 143
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7768916"
SQ SEQUENCE 335 AA; 37356 MW; FBAD1228C75F1CAF CRC64;
MKTANFSFAL CLSVVIMLFI KCTRSEQDLS VTKDAIAQKS GVTVSAVNLS NLIAYKNSDH
QISAGYYRTW RDSATASGNL PSMRWLPDSL DMVMVFPDYT PPENAYWNTL KTNYVPYLHK
RGTKVIITLG DLNSATTTGG QDSIGYSSWA KGIYDKWVGE YNLDGIDIDI ESSPSGATLT
KFVAATKALS KYFGPKSGTG KTFVYDTNQN PTNFFIQTAP RYNYVFLQAY GRSTTNLTTV
SGLYAPYISM KQFLPGFSFY EENGYPGNYW NDVRYPQNGT GRAYDYARWQ PATGKKGGVF
SYAIERDAPL TSSNDNTLRA PNFRVTKDLI KIMNP
