ProGP115

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ProGP ID ProGP115
Validation Status Characterized
Organism Information
Organism NameFlavobacterium 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
Protein Information
Protein NameFlavastacin (P40)
UniProtKB/SwissProt ID Q47899
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
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.
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 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 Logo
Technique(s) used for Glycosylation DetectionPhenol-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 ID137520
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
Additional CommentFlavastacin 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 Identification Month Wise1995.06.02
Year of Validation 1995
Reference 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]
Author Plummer, T.H., Jr.
Research GroupDivision of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.
Corresponding Author Tarentino, A.L., Quinones, G., Grimwood, B.G., Hauer, C.R. Plummer, T.H., Jr.
ContactDivision of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.
Reference1) 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]
Author Plummer, T.H., Jr., Tarentino, A.L. and Hauer, C.R.
Research GroupDivision of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.
Corresponding Author Hauer, C.R.
ContactDivision of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA.
Reference 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]
Author Reinhold, B.B., Hauer, C.R., Plummer, T.H. Reinhold, V.N.
Research GroupDepartment of Nutrition, Harvard University School of Public Health, Boston, Massachusetts 02115, USA.
Corresponding Author Reinhold, V.N.
ContactDepartment of Nutrition, Harvard University School of Public Health, Boston, Massachusetts 02115, USA.
Reference 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]
Author Reinhold, B.B., Hauer, C.R., Plummer, T.H. Reinhold, V.N.
Research GroupDepartment of Nutrition, Harvard University School of Public Health, Boston, Massachusetts 02115, USA
Corresponding Author Reinhold, V.N.
ContactDepartment of Nutrition, Harvard University School of Public Health, Boston, Massachusetts 02115, USA