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Protein

Pyrolysin

Gene

pls

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has endopeptidase activity toward caseins, casein fragments including alpha-S1-casein and synthetic peptides.

Temperature dependencei

Thermostable. Highly active at 95 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791Charge relay systemBy similarity
Active sitei365 – 3651Charge relay systemBy similarity
Active sitei590 – 5901Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.B55. 5243.

Protein family/group databases

MEROPSiS08.100.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrolysin (EC:3.4.21.-)
Gene namesi
Name:pls
Ordered Locus Names:PF0287
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Propeptidei27 – 1491231 PublicationPRO_0000027128Add
BLAST
Chaini150 – 13981249PyrolysinPRO_0000027129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi152 – 1521N-linked (GlcNAc...)
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence analysis
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence analysis
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence analysis
Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence analysis
Glycosylationi663 – 6631N-linked (GlcNAc...)Sequence analysis
Glycosylationi739 – 7391N-linked (GlcNAc...)Sequence analysis
Glycosylationi792 – 7921N-linked (GlcNAc...)Sequence analysis
Glycosylationi893 – 8931N-linked (GlcNAc...)Sequence analysis
Glycosylationi908 – 9081N-linked (GlcNAc...)Sequence analysis
Glycosylationi917 – 9171N-linked (GlcNAc...)Sequence analysis
Glycosylationi929 – 9291N-linked (GlcNAc...)Sequence analysis
Glycosylationi1048 – 10481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1056 – 10561N-linked (GlcNAc...)Sequence analysis
Glycosylationi1084 – 10841N-linked (GlcNAc...)Sequence analysis
Glycosylationi1117 – 11171N-linked (GlcNAc...)Sequence analysis
Glycosylationi1133 – 11331N-linked (GlcNAc...)Sequence analysis
Glycosylationi1140 – 11401N-linked (GlcNAc...)Sequence analysis
Glycosylationi1148 – 11481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1208 – 12081N-linked (GlcNAc...)Sequence analysis
Glycosylationi1233 – 12331N-linked (GlcNAc...)Sequence analysis
Glycosylationi1237 – 12371N-linked (GlcNAc...)Sequence analysis
Glycosylationi1332 – 13321N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

LWM pyrolysin seems to be produced by autoproteolytic activation of HMW pyrolysin.
Glycosylated.

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

PRIDEiP72186.

Interactioni

Protein-protein interaction databases

STRINGi186497.PF0287.

Structurei

3D structure databases

ProteinModelPortaliP72186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini174 – 380207Peptidase S8 1Add
BLAST
Domaini408 – 654247Peptidase S8 2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 2 peptidase S8 domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiarCOG00702. Archaea.
arCOG03610. Archaea.
COG1404. LUCA.
OMAiKIVDWVT.

Family and domain databases

Gene3Di3.40.50.200. 2 hits.
InterProiIPR007280. Peptidase_C_arc/bac.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 5 hits.
PfamiPF00082. Peptidase_S8. 2 hits.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 4 hits.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P72186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKKGLTVLF IAIMLLSVVP VHFVSAGTPP VSSENSTTSI LPNQQVVTKE
60 70 80 90 100
VSQAALNAIM KGQPNMVLII KTKEGKLEEA KTELEKLGAE ILDENRVLNM
110 120 130 140 150
LLVKIKPEKV KELNYISSLE KAWLNREVKL SPPIVEKDVK TKEPSLEPKM
160 170 180 190 200
YNSTWVINAL QFIQEFGYDG SGVVVAVLDT GVDPNHPFLS ITPDGRRKII
210 220 230 240 250
EWKDFTDEGF VDTSFSFSKV VNGTLIINTT FQVASGLTLN ESTGLMEYVV
260 270 280 290 300
KTVYVSNVTI GNITSANGIY HFGLLPERYF DLNFDGDQED FYPVLLVNST
310 320 330 340 350
GNGYDIAYVD TDLDYDFTDE VPLGQYNVTY DVAVFSYYYG PLNYVLAEID
360 370 380 390 400
PNGEYAVFGW DGHGHGTHVA GTVAGYDSNN DAWDWLSMYS GEWEVFSRLY
410 420 430 440 450
GWDYTNVTTD TVQGVAPGAQ IMAIRVLRSD GRGSMWDIIE GMTYAATHGA
460 470 480 490 500
DVISMSLGGN APYLDGTDPE SVAVDELTEK YGVVFVIAAG NEGPGINIVG
510 520 530 540 550
SPGVATKAIT VGAAAVPINV GVYVSQALGY PDYYGFYYFP AYTNVRIAFF
560 570 580 590 600
SSRGPRIDGE IKPNVVAPGY GIYSSLPMWI GGADFMSGTS MATPHVSGVV
610 620 630 640 650
ALLISGAKAE GIYYNPDIIK KVLESGATWL EGDPYTGQKY TELDQGHGLV
660 670 680 690 700
NVTKSWEILK AINGTTLPIV DHWADKSYSD FAEYLGVDVI RGLYARNSIP
710 720 730 740 750
DIVEWHIKYV GDTEYRTFEI YATEPWIKPF VSGSVILENN TEFVLRVKYD
760 770 780 790 800
VEGLEPGLYV GRIIIDDPTT PVIEDEILNT IVIPEKFTPE NNYTLTWYDI
810 820 830 840 850
NGPEMVTHHF FTVPEGVDVL YAMTTYWDYG LYRPDGMFVF PYQLDYLPAA
860 870 880 890 900
VSNPMPGNWE LVWTGFNFAP LYESGFLVRI YGVEITPSVW YINRTYLDTN
910 920 930 940 950
TEFSIEFNIT NIYAPINATL IPIGLGTYNA SVESVGDGEF FIKGIEVPEG
960 970 980 990 1000
TAELKIRIGN PSVPNSDLDL YLYDSKGNLV ALDGNPTAEE EVVVEYPKPG
1010 1020 1030 1040 1050
VYSIVVHGYS VRDENGNPTT TTFDLVVQMT LDNGNIKLDK DSIILGSNES
1060 1070 1080 1090 1100
VVVTANITID RDHPTGVYSG IIEIRDNEVY QDTNTSIAKI PITLVIDKAD
1110 1120 1130 1140 1150
FAVGLTPAEG VLGEARNYTL IVKHALTLEP VPNATVIIGN YTYLTDENGT
1160 1170 1180 1190 1200
VTFTYAPTKL GSDEITVIVK KENFNTLEKT FQITVSEPEI TEEDINEPKL
1210 1220 1230 1240 1250
AMSSPEANAT IVSVEMESEG GVKKTVTVEI TINGTANETA TIVVPVPKKA
1260 1270 1280 1290 1300
ENIEVSGDHV ISYSIEEGEY AKYVIITVKF ASPVTVTVTY TIYAGPRVSI
1310 1320 1330 1340 1350
LTLNFLGYSW YRLYSQKFDE LYQKALELGV DNETLALALS YHEKAKEYYE
1360 1370 1380 1390
KALELSEGNI IQYLGDIRLL PPLRQAYINE MKAVKILEKA IEELEGEE
Length:1,398
Mass (Da):154,475
Last modified:April 3, 2002 - v2
Checksum:i355D873A27D56552
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti607 – 6093AKA → PKP in AAB09761 (PubMed:8702780).Curated
Sequence conflicti881 – 8811Y → H in AAB09761 (PubMed:8702780).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55835 Genomic DNA. Translation: AAB09761.1.
AE009950 Genomic DNA. Translation: AAL80411.1.
PIRiT28159.
RefSeqiWP_011011401.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80411; AAL80411; PF0287.
GeneIDi1468121.
KEGGipfu:PF0287.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55835 Genomic DNA. Translation: AAB09761.1.
AE009950 Genomic DNA. Translation: AAL80411.1.
PIRiT28159.
RefSeqiWP_011011401.1. NC_003413.1.

3D structure databases

ProteinModelPortaliP72186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0287.

Protein family/group databases

MEROPSiS08.100.

Proteomic databases

PRIDEiP72186.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80411; AAL80411; PF0287.
GeneIDi1468121.
KEGGipfu:PF0287.

Phylogenomic databases

eggNOGiarCOG00702. Archaea.
arCOG03610. Archaea.
COG1404. LUCA.
OMAiKIVDWVT.

Enzyme and pathway databases

BRENDAi3.4.21.B55. 5243.

Family and domain databases

Gene3Di3.40.50.200. 2 hits.
InterProiIPR007280. Peptidase_C_arc/bac.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 5 hits.
PfamiPF00082. Peptidase_S8. 2 hits.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 4 hits.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus."
    Voorhorst W.G.B., Eggen R.I.L., Geerling A.C.M., Platteeuw C., Siezen R.J., de Vos W.M.
    J. Biol. Chem. 271:20426-20431(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 150-184, CHARACTERIZATION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "Purification, characterization, and molecular modeling of pyrolysin and other extracellular thermostable serine proteases from hyperthermophilic microorganisms."
    de Vos W.M., Voorhorst W.G.B., Dijkgraaf M., Kluskens L.D., Van der Oost J., Siezen R.J.
    Methods Enzymol. 330:383-393(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiPLS_PYRFU
AccessioniPrimary (citable) accession number: P72186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: April 3, 2002
Last modified: May 11, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.