ProGlyProt ID BC143 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 L37784 Gene Information Gene Name NCBI Gene ID Protein Information Protein Name Flavastacin (P40) UniProtKB/SwissProt ID Q47899 NCBI RefSeq EMBL-CDS AAC41455.1 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 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 PDB ID 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 MTRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNG EYFYADDITITAEQFNQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQ AYNTFLTNINKAFDMISSKTSVKFVQRTNQTEYITFTYSTGNSSPLGWVKNRVNGIKIYN TTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRHNFNLYNDYAGHGEFDFG SVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNGTYT LTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDS*(355)TKVLT VRNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPI VIGSTDQTLQPYTKQRFTLTKVN Sequence Around Glycosites (21 AA) GYFTIKSILDSTKVLTVRNNG Glycosite Sequence Logo seqlogo Glycosite Sequence Logo 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]. 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 Flavastacin 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 Identification 1995 Year of Validation 1995