PLS_PYRFU
ID PLS_PYRFU Reviewed; 1398 AA.
AC P72186;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pyrolysin;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=pls; OrderedLocusNames=PF0287;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 150-184, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8702780; DOI=10.1074/jbc.271.34.20426;
RA Voorhorst W.G.B., Eggen R.I.L., Geerling A.C.M., Platteeuw C., Siezen R.J.,
RA de Vos W.M.;
RT "Isolation and characterization of the hyperthermostable serine protease,
RT pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus
RT furiosus.";
RL J. Biol. Chem. 271:20426-20431(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP CHARACTERIZATION, AND 3D-STRUCTURE MODELING.
RX PubMed=11210516; DOI=10.1016/s0076-6879(01)30390-7;
RA de Vos W.M., Voorhorst W.G.B., Dijkgraaf M., Kluskens L.D.,
RA Van der Oost J., Siezen R.J.;
RT "Purification, characterization, and molecular modeling of pyrolysin and
RT other extracellular thermostable serine proteases from hyperthermophilic
RT microorganisms.";
RL Methods Enzymol. 330:383-393(2001).
CC -!- FUNCTION: Has endopeptidase activity toward caseins, casein fragments
CC including alpha-S1-casein and synthetic peptides.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. Highly active at 95 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: Cell envelope. Note=Cell envelope associated.
CC -!- PTM: LWM pyrolysin seems to be produced by autoproteolytic activation
CC of HMW pyrolysin.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; U55835; AAB09761.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80411.1; -; Genomic_DNA.
DR PIR; T28159; T28159.
DR RefSeq; WP_011011401.1; NZ_CP023154.1.
DR AlphaFoldDB; P72186; -.
DR SMR; P72186; -.
DR STRING; 186497.PF0287; -.
DR MEROPS; S08.100; -.
DR PRIDE; P72186; -.
DR EnsemblBacteria; AAL80411; AAL80411; PF0287.
DR GeneID; 41712077; -.
DR KEGG; pfu:PF0287; -.
DR PATRIC; fig|186497.12.peg.299; -.
DR eggNOG; arCOG00704; Archaea.
DR eggNOG; arCOG03610; Archaea.
DR HOGENOM; CLU_264582_0_0_2; -.
DR OMA; WVTATDP; -.
DR OrthoDB; 53822at2157; -.
DR BRENDA; 3.4.21.B55; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; -; 2.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..149
FT /evidence="ECO:0000269|PubMed:8702780"
FT /id="PRO_0000027128"
FT CHAIN 150..1398
FT /note="Pyrolysin"
FT /id="PRO_0000027129"
FT DOMAIN 154..656
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 590
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1056
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1084
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 607..609
FT /note="AKA -> PKP (in Ref. 1; AAB09761)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="Y -> H (in Ref. 1; AAB09761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1398 AA; 154475 MW; 355D873A27D56552 CRC64;
MNKKGLTVLF IAIMLLSVVP VHFVSAGTPP VSSENSTTSI LPNQQVVTKE VSQAALNAIM
KGQPNMVLII KTKEGKLEEA KTELEKLGAE ILDENRVLNM LLVKIKPEKV KELNYISSLE
KAWLNREVKL SPPIVEKDVK TKEPSLEPKM YNSTWVINAL QFIQEFGYDG SGVVVAVLDT
GVDPNHPFLS ITPDGRRKII EWKDFTDEGF VDTSFSFSKV VNGTLIINTT FQVASGLTLN
ESTGLMEYVV KTVYVSNVTI GNITSANGIY HFGLLPERYF DLNFDGDQED FYPVLLVNST
GNGYDIAYVD TDLDYDFTDE VPLGQYNVTY DVAVFSYYYG PLNYVLAEID PNGEYAVFGW
DGHGHGTHVA GTVAGYDSNN DAWDWLSMYS GEWEVFSRLY GWDYTNVTTD TVQGVAPGAQ
IMAIRVLRSD GRGSMWDIIE GMTYAATHGA DVISMSLGGN APYLDGTDPE SVAVDELTEK
YGVVFVIAAG NEGPGINIVG SPGVATKAIT VGAAAVPINV GVYVSQALGY PDYYGFYYFP
AYTNVRIAFF SSRGPRIDGE IKPNVVAPGY GIYSSLPMWI GGADFMSGTS MATPHVSGVV
ALLISGAKAE GIYYNPDIIK KVLESGATWL EGDPYTGQKY TELDQGHGLV NVTKSWEILK
AINGTTLPIV DHWADKSYSD FAEYLGVDVI RGLYARNSIP DIVEWHIKYV GDTEYRTFEI
YATEPWIKPF VSGSVILENN TEFVLRVKYD VEGLEPGLYV GRIIIDDPTT PVIEDEILNT
IVIPEKFTPE NNYTLTWYDI NGPEMVTHHF FTVPEGVDVL YAMTTYWDYG LYRPDGMFVF
PYQLDYLPAA VSNPMPGNWE LVWTGFNFAP LYESGFLVRI YGVEITPSVW YINRTYLDTN
TEFSIEFNIT NIYAPINATL IPIGLGTYNA SVESVGDGEF FIKGIEVPEG TAELKIRIGN
PSVPNSDLDL YLYDSKGNLV ALDGNPTAEE EVVVEYPKPG VYSIVVHGYS VRDENGNPTT
TTFDLVVQMT LDNGNIKLDK DSIILGSNES VVVTANITID RDHPTGVYSG IIEIRDNEVY
QDTNTSIAKI PITLVIDKAD FAVGLTPAEG VLGEARNYTL IVKHALTLEP VPNATVIIGN
YTYLTDENGT VTFTYAPTKL GSDEITVIVK KENFNTLEKT FQITVSEPEI TEEDINEPKL
AMSSPEANAT IVSVEMESEG GVKKTVTVEI TINGTANETA TIVVPVPKKA ENIEVSGDHV
ISYSIEEGEY AKYVIITVKF ASPVTVTVTY TIYAGPRVSI LTLNFLGYSW YRLYSQKFDE
LYQKALELGV DNETLALALS YHEKAKEYYE KALELSEGNI IQYLGDIRLL PPLRQAYINE
MKAVKILEKA IEELEGEE
