ProGlyProt IDBC143
Organism Information
Organism NameFlavobacterium meningosepticum (Elizabethkingia meningoseptica)
DomainBacteria
ClassificationFamily: Flavobacteriaceae
Order: "Flavobacteriales"
Class: Flavobacteria
Division or phylum: "Bacteroidetes"
Taxonomic ID (NCBI)238
Genome Sequence (s)
EMBLL37784
Gene Information
Gene Name
NCBI Gene ID
Protein Information
Protein NameFlavastacin (P40)
UniProtKB/SwissProt IDQ47899
NCBI RefSeq
EMBL-CDSAAC41455.1
UniProtKB Sequence>sp|Q47899|FLVS_FLAME Flavastacin OS=Flavobacterium meningosepticum PE=1 SV=1 MTRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNG EYFYADDITITAEQFNQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQ AYNTFLTNINKAFDMISSKTSVKFVQRTNQTEYITFTYSTGNSSPLGWVKNRVNGIKIYN TTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRHNFNLYNDYAGHGEFDFG SVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNGTYT LTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDSTKVLT VRNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPI VIGSTDQTLQPYTKQRFTLTKVN
Sequence length 443 AA
Subcellular LocationPeriplasm
FunctionZinc 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
PDB ID
Glycosylation Status
Glycosylation TypeO (Ser) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide: 1-15, propeptide: 15-91) S355
Experimentally Validated Glycosite(s ) in Mature ProteinS264
Glycosite(s) Annotated Protein Sequence>sp|Q47899|FLVS_FLAME Flavastacin OS=Flavobacterium meningosepticum PE=1 SV=1 MTRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNG EYFYADDITITAEQFNQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQ AYNTFLTNINKAFDMISSKTSVKFVQRTNQTEYITFTYSTGNSSPLGWVKNRVNGIKIYN TTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRHNFNLYNDYAGHGEFDFG SVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNGTYT LTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDS*(355)TKVLT VRNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPI VIGSTDQTLQPYTKQRFTLTKVN
Sequence Around Glycosites (21 AA)GYFTIKSILDSTKVLTVRNNG
Glycosite Sequence Logoseqlogo
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionPhenol-sulfuric acid assay
Technique(s) used for Glycosylated Residue(s) DetectionCollision activated dissociation (CAD) mass spectrometry and Edman degradation
Protein Glycosylation- ImplicationGlycosylation may contribute towards protein stability
Glycan Information
Glycan AnnotationLinkage: 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].
Technique(s) used for Glycan IdentificationESI-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 LinksCAZy
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 CommentsFlavastacin is the first example of a prokaryotic enzyme related to the eukaryotic astacin group.
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.
Year of Identification1995
Year of Validation1995