ID   SEPR_THESR              Reviewed;         410 AA.
AC   P80146;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Extracellular serine proteinase;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Thermus sp. (strain Rt41A).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus;
OC   unclassified Thermus.
OX   NCBI_TaxID=32063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7551039; DOI=10.1099/13500872-141-7-1731;
RA   Munro G.K., McHale R.H., Saul D.J., Reeves R.A., Bergquist P.L.;
RT   "A gene encoding a thermophilic alkaline serine proteinase from Thermus sp.
RT   strain Rt41A and its expression in Escherichia coli.";
RL   Microbiology 141:1731-1738(1995).
RN   [2]
RP   SEQUENCE REVISION TO 34-120.
RA   Gibbs M.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 133-147, AND CHARACTERIZATION.
RX   PubMed=1499549; DOI=10.1111/j.1432-1033.1992.tb17140.x;
RA   Peek K., Daniel R.M., Monk C., Parker L., Coolbear T.;
RT   "Purification and characterization of a thermostable proteinase isolated
RT   from Thermus sp. strain Rt41A.";
RL   Eur. J. Biochem. 207:1035-1044(1992).
CC   -!- FUNCTION: Serine proteinase with preferred activity for amino acids
CC       with aromatic side groups at the P1' side of the scissible bond.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Contains 4 Cys residues that form two disulfide bonds.
CC   -!- PTM: Glycosylated. This proteinase has a 0.7% carbohydrate content.
CC       {ECO:0000269|PubMed:1499549}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; U17342; AAA82980.2; -; Genomic_DNA.
DR   AlphaFoldDB; P80146; -.
DR   SMR; P80146; -.
DR   MEROPS; S08.008; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
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   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 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; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..132
FT                   /evidence="ECO:0000269|PubMed:1499549"
FT                   /id="PRO_0000027161"
FT   CHAIN           133..410
FT                   /note="Extracellular serine proteinase"
FT                   /id="PRO_0000027162"
FT   DOMAIN          45..130
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          139..410
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        356
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   410 AA;  42876 MW;  9A2445F47F0C23D5 CRC64;
     MKRGGLWLLL GLLVLSACSS NPPAASTQEA PLLGLEAPEA IPGRYIVVYK ENADVLPALE
     ALKAALEPGL MQPQGLQAQA LRTLGLEGAR VDKVYTAALR GVAVEVPDQE LARLRQDPRV
     AYIEADQEVR AFAVQSPATW GLDRIDQRTL PLDGRYTYTA TGAGVHAYVV DTGILLSHQE
     FTGRIGKGYD AITPGGSAQD CNGHGTHVAG TIGGTTYGVA KGVTLHPVRV LDCNGSGSNS
     SVIAGLDWVT QNHVKPAVIN MSLGGGASTA LDTAVMNAIN AGVTVVVAAG NDNRDACFYS
     PARVTAAITV GATTSTDYRA SFSNYGRCLD LFAPGQSITS AWYTSSTATN TISGTSMATP
     HVTGAAALYL QWYPTATPSQ VASALLYYAT PNVVKNAGRY SPNLLLYTPF