ProGP130 (Pyrolysin)
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| ProGP ID | ProGP130 (Pyrolysin) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Pyrococcus furiosus DSM 3638 |
| Domain | Archaea |
| Classification | Family: Thermococcaceae Order: Thermococcales Class: Thermococci or Protoarchaea Division or phylum: "Euryarchaeota" |
| Taxonomic ID (NCBI) | 2261 |
| Genome Information | |
| GenBank | AE009950.1 |
| EMBL | AE009950 |
| Gene Information | |
| Gene Name | pls (PF0287) |
| NCBI Gene ID | 1468121 |
| GenBank Gene Sequence | NC_003413 |
| Protein Information | |
| Protein Name | Pyrolysin |
| UniProtKB/SwissProt ID | P72186 |
| NCBI RefSeq | NP_578016.1 |
| EMBL-CDS | AAL80411.1 |
| 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 Location | Cell 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 Protein | N3 |
| 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 |
| Technique(s) used for Glycosylation Detection | Periodic 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 Name | AglB/STT3 |
| OST ProGT ID | ProGT23 (AglB) |
| Literature | |
| Reference | Igura, M. and Kohda, D., 2011. Selective control of oligosaccharide transfer efficiency for the N-glycosylation sequon by a point mutation in oligosaccharyltransferase. Journal of Biological Chemistry, 286(15), pp.13255-13260. |
| Corresponding Author | Daisuke Kohda |
| Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
| Reference | de 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. In Methods in enzymology (Vol. 330, pp. 383-393). Academic Press. |
| Contact | Laboratory 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 de Vos, W.M., 1996. Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus. Journal of Biological Chemistry, 271(34), pp.20426-20431. |
| Corresponding Author | Willem M.de Vos |
| Contact | Department of Microbiology, Wageningen Agricultural University, 6703 CT Wageningen. |
| 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] |
| Corresponding Author | Daisuke Kohda |
| Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
| Reference | Igura, 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 Group | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
| Corresponding Author | Kohda, D. |
| Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, 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. and Kohda, D. |
| Research Group | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan. |
| Corresponding Author | Kohda, D. |
| Contact | Division 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 Group | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan. |
| Corresponding Author | Kohda, D. |
| Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan. |
| Reference | de 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 Group | Laboratory of Microbiology, Wageningen Agricultural University, Wageningen, NL-6703 CT, The Netherlands. |
| Corresponding Author | Siezen, R.J. |
| Contact | Laboratory 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 Group | Department of Microbiology, Wageningen Agricultural University, 6703 CT Wageningen. |
| Corresponding Author | Vos, W.M. |
| Contact | Department of Microbiology, Wageningen Agricultural University, 6703 CT Wageningen. |