P36912 (EBA2_FLAME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-beta-N-acetylglucosaminidase F2
EC=3.2.1.96

Alternative name(s):
Di-N-acetylchitobiosyl beta-N-acetylglucosaminidase F2
Endoglycosidase F2
Mannosyl-glycoprotein endo-beta-N-acetyl-glucosaminidase F2

Gene names

Name:

endOF2

Organism

Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)

Taxonomic identifier

238 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Complex biantennary glycans are the preferred substrates. Tri- and tetraantennary glycans are not hydrolyzed, and high mannose glycans are very poor substrates.
Catalytic activity	Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Subunit structure	Monomer.
Subcellular location	Secreted.
Post-translational modification	Carbohydrates at Ser-73, Ser-89 and Ser-143 consist of (2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU1-4[(2-OMe)Rham1-2]Man.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 45	45
	Chain	46 – 335	290	Endo-beta-N-acetylglucosaminidase F2		PRO_0000011956
Sites
	Active site	171	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	73	1	O-linked (Man...) Ref.2
	Glycosylation	89	1	O-linked (Man...) Ref.2
	Glycosylation	143	1	O-linked (Man...) Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P36912 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: FBAD1228C75F1CAF	FASTA	335	37,356
	10 20 30 40 50 60 MKTANFSFAL CLSVVIMLFI KCTRSEQDLS VTKDAIAQKS GVTVSAVNLS NLIAYKNSDH 70 80 90 100 110 120 QISAGYYRTW RDSATASGNL PSMRWLPDSL DMVMVFPDYT PPENAYWNTL KTNYVPYLHK 130 140 150 160 170 180 RGTKVIITLG DLNSATTTGG QDSIGYSSWA KGIYDKWVGE YNLDGIDIDI ESSPSGATLT 190 200 210 220 230 240 KFVAATKALS KYFGPKSGTG KTFVYDTNQN PTNFFIQTAP RYNYVFLQAY GRSTTNLTTV 250 260 270 280 290 300 SGLYAPYISM KQFLPGFSFY EENGYPGNYW NDVRYPQNGT GRAYDYARWQ PATGKKGGVF 310 320 330 SYAIERDAPL TSSNDNTLRA PNFRVTKDLI KIMNP

References

[1]	"Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression." Tarentino A.L., Quinones G., Changchien L.-M., Plummer T.H. Jr. J. Biol. Chem. 268:9702-9708(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Novel, specific O-glycosylation of secreted Flavobacterium meningosepticum proteins. Asp-Ser and Asp-Thr-Thr consensus sites." Plummer T.H. Jr., Tarentino A.L., Hauer C.R. J. Biol. Chem. 270:13192-13196(1995) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-73; SER-89 AND SER-143, MASS SPECTROMETRY.
[3]	"Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum." Reinhold B.B., Hauer C.R., Plummer T.H. Jr., Reinhold V.N. J. Biol. Chem. 270:13197-13203(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06331 Genomic DNA. Translation: AAA24923.1.
PIR	A46678.
3D structure databases
ProteinModelPortal	P36912.
ModBase	Search...
Protein family/group databases
CAZy	GH18. Glycoside Hydrolase Family 18.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001579. Glyco_hydro_18_chit_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS01095. CHITINASE_18. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EBA2_FLAME

Accession

Primary (citable) accession number: P36912

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program