ProGP130

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ProGP ID ProGP130
Validation Status Characterized
Organism Information
Organism NamePyrococcus furiosus DSM 3638
Domain Archaea
Classification Family: Thermococcaceae
Order: Thermococcales
Class: Thermococci or Protoarchaea
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI) 2261
Genome Sequence(s)
GenBank AE009950.1
EMBL AE009950
Gene Information
Gene Namepls (PF0287)
NCBI Gene ID 1468121
GenBank Gene Sequence 1468121
Protein Information
Protein NamePyrolysin
UniProtKB/SwissProt ID P72186
NCBI RefSeq NP_578016.1
EMBL-CDSAAL80411.1
UniProtKB Sequence >sp|P72186|PLS_PYRFU Pyrolysin OS=Pyrococcus furiosus GN=pls PE=1 SV=2 MNKKGLTVLFIAIMLLSVVPVHFVSAGTPPVSSENSTTSILPNQQVVTKEVSQAALNAIM KGQPNMVLIIKTKEGKLEEAKTELEKLGAEILDENRVLNMLLVKIKPEKVKELNYISSLE KAWLNREVKLSPPIVEKDVKTKEPSLEPKMYNSTWVINALQFIQEFGYDGSGVVVAVLDT GVDPNHPFLSITPDGRRKIIEWKDFTDEGFVDTSFSFSKVVNGTLIINTTFQVASGLTLN ESTGLMEYVVKTVYVSNVTIGNITSANGIYHFGLLPERYFDLNFDGDQEDFYPVLLVNST GNGYDIAYVDTDLDYDFTDEVPLGQYNVTYDVAVFSYYYGPLNYVLAEIDPNGEYAVFGW DGHGHGTHVAGTVAGYDSNNDAWDWLSMYSGEWEVFSRLYGWDYTNVTTDTVQGVAPGAQ IMAIRVLRSDGRGSMWDIIEGMTYAATHGADVISMSLGGNAPYLDGTDPESVAVDELTEK YGVVFVIAAGNEGPGINIVGSPGVATKAITVGAAAVPINVGVYVSQALGYPDYYGFYYFP AYTNVRIAFFSSRGPRIDGEIKPNVVAPGYGIYSSLPMWIGGADFMSGTSMATPHVSGVV ALLISGAKAEGIYYNPDIIKKVLESGATWLEGDPYTGQKYTELDQGHGLVNVTKSWEILK AINGTTLPIVDHWADKSYSDFAEYLGVDVIRGLYARNSIPDIVEWHIKYVGDTEYRTFEI YATEPWIKPFVSGSVILENNTEFVLRVKYDVEGLEPGLYVGRIIIDDPTTPVIEDEILNT IVIPEKFTPENNYTLTWYDINGPEMVTHHFFTVPEGVDVLYAMTTYWDYGLYRPDGMFVF PYQLDYLPAAVSNPMPGNWELVWTGFNFAPLYESGFLVRIYGVEITPSVWYINRTYLDTN TEFSIEFNITNIYAPINATLIPIGLGTYNASVESVGDGEFFIKGIEVPEGTAELKIRIGN PSVPNSDLDLYLYDSKGNLVALDGNPTAEEEVVVEYPKPGVYSIVVHGYSVRDENGNPTT TTFDLVVQMTLDNGNIKLDKDSIILGSNESVVVTANITIDRDHPTGVYSGIIEIRDNEVY QDTNTSIAKIPITLVIDKADFAVGLTPAEGVLGEARNYTLIVKHALTLEPVPNATVIIGN YTYLTDENGTVTFTYAPTKLGSDEITVIVKKENFNTLEKTFQITVSEPEITEEDINEPKL AMSSPEANATIVSVEMESEGGVKKTVTVEITINGTANETATIVVPVPKKAENIEVSGDHV ISYSIEEGEYAKYVIITVKFASPVTVTVTYTIYAGPRVSILTLNFLGYSWYRLYSQKFDE LYQKALELGVDNETLALALSYHEKAKEYYEKALELSEGNIIQYLGDIRLLPPLRQAYINE MKAVKILEKAIEELEGEE
Sequence length 1398 AA
Subcellular LocationCell envelope associated
Function Hyperthermostable serine protease. Has endopeptidase activity toward caseins, casein fragments including alpha-S1-casein and synthetic peptides. EC= 3.1.21.-
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide: 1-26, propeptide: 26-149) N152
Experimentally Validated Glycosite(s ) in Mature ProteinN3
Glycosite(s) Annotated Protein Sequence >sp|P72186|PLS_PYRFU Pyrolysin OS=Pyrococcus furiosus GN=pls PE=1 SV=2 MNKKGLTVLFIAIMLLSVVPVHFVSAGTPPVSSENSTTSILPNQQVVTKEVSQAALNAIM KGQPNMVLIIKTKEGKLEEAKTELEKLGAEILDENRVLNMLLVKIKPEKVKELNYISSLE KAWLNREVKLSPPIVEKDVKTKEPSLEPKMYN*(152)STWVINALQFIQEFGYDGSGVVVAVLDT GVDPNHPFLSITPDGRRKIIEWKDFTDEGFVDTSFSFSKVVNGTLIINTTFQVASGLTLN ESTGLMEYVVKTVYVSNVTIGNITSANGIYHFGLLPERYFDLNFDGDQEDFYPVLLVNST GNGYDIAYVDTDLDYDFTDEVPLGQYNVTYDVAVFSYYYGPLNYVLAEIDPNGEYAVFGW DGHGHGTHVAGTVAGYDSNNDAWDWLSMYSGEWEVFSRLYGWDYTNVTTDTVQGVAPGAQ IMAIRVLRSDGRGSMWDIIEGMTYAATHGADVISMSLGGNAPYLDGTDPESVAVDELTEK YGVVFVIAAGNEGPGINIVGSPGVATKAITVGAAAVPINVGVYVSQALGYPDYYGFYYFP AYTNVRIAFFSSRGPRIDGEIKPNVVAPGYGIYSSLPMWIGGADFMSGTSMATPHVSGVV ALLISGAKAEGIYYNPDIIKKVLESGATWLEGDPYTGQKYTELDQGHGLVNVTKSWEILK AINGTTLPIVDHWADKSYSDFAEYLGVDVIRGLYARNSIPDIVEWHIKYVGDTEYRTFEI YATEPWIKPFVSGSVILENNTEFVLRVKYDVEGLEPGLYVGRIIIDDPTTPVIEDEILNT IVIPEKFTPENNYTLTWYDINGPEMVTHHFFTVPEGVDVLYAMTTYWDYGLYRPDGMFVF PYQLDYLPAAVSNPMPGNWELVWTGFNFAPLYESGFLVRIYGVEITPSVWYINRTYLDTN TEFSIEFNITNIYAPINATLIPIGLGTYNASVESVGDGEFFIKGIEVPEGTAELKIRIGN PSVPNSDLDLYLYDSKGNLVALDGNPTAEEEVVVEYPKPGVYSIVVHGYSVRDENGNPTT TTFDLVVQMTLDNGNIKLDKDSIILGSNESVVVTANITIDRDHPTGVYSGIIEIRDNEVY QDTNTSIAKIPITLVIDKADFAVGLTPAEGVLGEARNYTLIVKHALTLEPVPNATVIIGN YTYLTDENGTVTFTYAPTKLGSDEITVIVKKENFNTLEKTFQITVSEPEITEEDINEPKL AMSSPEANATIVSVEMESEGGVKKTVTVEITINGTANETATIVVPVPKKAENIEVSGDHV ISYSIEEGEYAKYVIITVKFASPVTVTVTYTIYAGPRVSILTLNFLGYSWYRLYSQKFDE LYQKALELGVDNETLALALSYHEKAKEYYEKALELSEGNIIQYLGDIRLLPPLRQAYINE MKAVKILEKAIEELEGEE
Sequence Around Glycosites (21 AA) KEPSLEPKMYNSTWVINALQF
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionPeriodic acid-Schiff (PAS) staining
Technique(s) used for Glycosylated Residue(s) Detection Edman degradation
Protein Glycosylation- Implication The post-translational modification may function in the thermostabilization of the enzyme.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAglB/STT3
OST ProGT IDProGT20
Literature
Year of Identification1996
Year of Identification Month Wise1996.8.23
Year of Validation 1996
ReferenceIgura, M. and Kohda, D. (2011) Selective control of oligosaccharide transfer efficiency for the N-glycosylation sequon by a point mutation in oligosaccharyltransferase. J Biol Chem, 286, 13255-13260. [PubMed: 21357684]
Author Igura, M. and Kohda, D.
Research GroupDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
Corresponding Author Kohda, D.
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
ReferenceIgura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K. and Kohda, D. (2008) Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J, 27, 234-243. [PubMed: 18046457]
Author Igura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K. and Kohda, D.
Research GroupDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Corresponding Author Kohda, D.
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Reference Igura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K. and Kohda, D. (2008) Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J, 27, 234-243. [PubMed: 18046457]
Author Igura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K. Kohda, D.
Research GroupDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Corresponding Author Kohda, D.
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Referencede Vos, W.M., Voorhorst, W.G., Dijkgraaf, M., Kluskens, L.D., Van der Oost, J. and Siezen, R.J. (2001) Purification, characterization, and molecular modeling of pyrolysin and other extracellular thermostable serine proteases from hyperthermophilic microorganisms. Methods Enzymol, 330, 383-393. [PubMed: 11210516]
Author de Vos, W.M., Voorhorst, W.G., Dijkgraaf, M., Kluskens, L.D., Van der Oost, J. Siezen, R.J.
Research GroupLaboratory of Microbiology, Wageningen Agricultural University, Wageningen, NL-6703 CT, The Netherlands.
Corresponding Author Siezen, R.J.
ContactLaboratory of Microbiology, Wageningen Agricultural University, Wageningen, NL-6703 CT, The Netherlands.
Reference Voorhorst, W.G., Eggen, R.I., Geerling, A.C., Platteeuw, C., Siezen, R.J. and Vos, W.M. (1996) Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem, 271, 20426-20431. [PubMed: 8702780]
Author Voorhorst, W.G., Eggen, R.I., Geerling, A.C., Platteeuw, C., Siezen, R.J. Vos, W.M.
Research GroupDepartment of Microbiology, Wageningen Agricultural University, 6703 CT Wageningen.
Corresponding Author Vos, W.M.
ContactDepartment of Microbiology, Wageningen Agricultural University, 6703 CT Wageningen.