ID   THPS_SULAC              Reviewed;         340 AA.
AC   P17118; Q4J861;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Thermopsin;
DE            EC=3.4.23.42;
DE   Flags: Precursor;
GN   Name=thpS; OrderedLocusNames=Saci_1714;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 42-76.
RX   PubMed=2104843; DOI=10.1016/s0021-9258(19)40043-4;
RA   Lin X.-L., Tang J.;
RT   "Purification, characterization, and gene cloning of thermopsin, a
RT   thermostable acid protease from Sulfolobus acidocaldarius.";
RL   J. Biol. Chem. 265:1490-1495(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: May represent a new class of acid proteases. It digests
CC       proteins and peptides in acidic solution.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specificity similar to pepsin A, prefers bulky hydrophobic
CC         side-chains on either side of the scissible bond.; EC=3.4.23.42;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 2.;
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius. Thermostable.;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=May be linked to cells by covalent
CC       linkages through some side chains.
CC   -!- SIMILARITY: Belongs to the peptidase A5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY81020.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; J05184; AAA72221.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY81020.1; ALT_INIT; Genomic_DNA.
DR   PIR; A35009; A35009.
DR   RefSeq; WP_015385662.1; NC_007181.1.
DR   AlphaFoldDB; P17118; -.
DR   MEROPS; A05.001; -.
DR   EnsemblBacteria; AAY81020; AAY81020; Saci_1714.
DR   GeneID; 3474479; -.
DR   KEGG; sai:Saci_1714; -.
DR   PATRIC; fig|330779.12.peg.1651; -.
DR   eggNOG; arCOG03674; Archaea.
DR   HOGENOM; CLU_815398_0_0_2; -.
DR   BRENDA; 3.4.23.42; 6160.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR007981; Peptidase_A5.
DR   Pfam; PF05317; Thermopsin; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..41
FT                   /evidence="ECO:0000269|PubMed:2104843"
FT                   /id="PRO_0000028499"
FT   CHAIN           42..340
FT                   /note="Thermopsin"
FT                   /id="PRO_0000028500"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
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        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   340 AA;  37262 MW;  E2758C0BC287FCE1 CRC64;
     MNFKSICLII LLSALIIPYI PQNIYFFPHR NTTGATISSG LYVNPYLYYT SPPAPAGIAS
     FGLYNYSGNV TPYVITTNEM LGYVNITSLL AYNREALRYG VDPYSATLQF NIVLSVNTSN
     GVYAYWLQDV GQFQTNKNSL TFIDNVWNLT GSLSTLSSSA ITGNGQVASA GGGQTFYYDV
     GPSYTYSFPL SYIYIINMSY TSNAVYVWIG YEIIQIGQTE YGTVNYYDKI TIYQPNIISA
     SLMINGNNYT PNGLYYDAEL VWGGGGNGAP TSFNSLNCTL GLYYISNGSI TPVPSLYTFG
     ADTAEAAYNV YTTMNNGVPI AYNGIENLTI LTNNFSVILI