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. 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. |