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ProGlyProt ID
BC143
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
 
 
Protein Information
Protein Name
Flavastacin (P40)
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
Sequence length
443 AA
Subcellular Location
Periplasm
Function
Zinc metalloendopeptidase (Zinc-aspartyl endoprotease) of astacin family that cleaves peptides on the amino-terminal side of aspartic acid. EC= 3.4.24.76., these enzymes are involved in extracellular matrix formation, morphogenesis and digestion.
 
 
Protein Structure
Homology Model
Homology Model File
 
 
Glycosylation Status
Glycosylation Type
O (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein
(Signal peptide: 1-15, propeptide: 15-91) S355
Experimentally Validated Glycosite(s ) in Mature Protein
S264
Glycosite(s) Annotated Protein Sequence
>sp|Q47899|FLVS_FLAME Flavastacin OS=Flavobacterium meningosepticum PE=1 SV=1 M
TRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNG EYFYADDITITAEQF
NQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQ AYNTFLTNINKAFDMISSKTSVKFVQRTN
QTEYITFTYSTGNSSPLGWVKNRVNGIKIYN TTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRH
NFNLYNDYAGHGEFDFG SVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNG
TYT LTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDS*(355)TKVLT V
RNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPI VIGSTDQTLQPYTKQ
RFTLTKVN
Sequence Around Glycosites (21 AA)
GYFTIKSILDSTKVLTVRNNG
Technique(s) used for Glycosylation Detection
Phenol-sulfuric acid assay
Technique(s) used for Glycosylated Residue(s) Detection
Collision activated dissociation (CAD) mass spectrometry and Edman degradation
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, 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) 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, A.L., Quinones, G., Grimwood, B.G., Hauer, C.R. and Plummer, T.H., Jr. (1995) Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase. Arch Biochem Biophys, 319, 281-285. [PubMed: 7771796]
Additional Comments
Flavastacin is the first example of a prokaryotic enzyme related to the eukaryotic astacin group.
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.
Year of Identification
1995
Year of Validation
1995
 
 
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