ID   SUBT_BACS9              Reviewed;         420 AA.
AC   P28842;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Subtilisin;
DE            EC=3.4.21.62;
DE   Flags: Precursor;
GN   Name=sub1;
OS   Bacillus sp. (strain TA39).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=29336;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1581352; DOI=10.1016/0167-4781(92)90108-c;
RA   Narinx E., Davail S., Feller G., Gerday C.;
RT   "Nucleotide and derived amino acid sequence of the subtilisin from the
RT   antarctic psychrotroph Bacillus TA39.";
RL   Biochim. Biophys. Acta 1131:111-113(1992).
CC   -!- FUNCTION: Subtilisin is an extracellular alkaline serine protease, it
CC       catalyzes the hydrolysis of proteins and peptide amides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds, and a preference for a large uncharged residue in P1.
CC         Hydrolyzes peptide amides.; EC=3.4.21.62;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Still active at temperatures close to 0 degrees Celsius.
CC         Thermolabile.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Secretion of subtilisin is associated with onset of
CC       sporulation, and many mutations which block sporulation at early stages
CC       affect expression levels of subtilisin. However, subtilisin is not
CC       necessary for normal sporulation.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; X62369; CAA44227.1; -; Genomic_DNA.
DR   PIR; S23407; S23407.
DR   AlphaFoldDB; P28842; -.
DR   SMR; P28842; -.
DR   MEROPS; S08.140; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; -; 1.
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   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   Calcium; Hydrolase; Metal-binding; Protease; Secreted; Serine protease;
KW   Signal; Sporulation; Zymogen.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   PROPEP          32..111
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027181"
FT   CHAIN           112..420
FT                   /note="Subtilisin"
FT                   /id="PRO_0000027182"
FT   DOMAIN          118..420
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        145
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        360
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   BINDING         115
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   420 AA;  44087 MW;  AE4F121BD32B26EC CRC64;
     MKRSGKIFTT AMLAVTLMMP AMGVSANEGN AAAEGNEKFR VLVDSVDQKN LKNAKQQYGV
     HWDFAGEGFT TDMNEKQFNA LKKNKNLTVE KVPELEIATA TDKPEALYNA MAASQSTPWG
     IKAIYNNSSI TQTSGGGGIN IAVLDTGVNT NHPDLRNNVE QCKDFTVGTT YTNNSCTDRQ
     GHGTHVAGSA LADGGTGNGV YGVAPDADLW AYKVLGDDGS GYADDIAAAI RHAGDQATAL
     NTKVVINMSL GSSGESSLIT NAVNYSYNKG VLIIAAAGNS GPYQGSIGYP GALVNAVAVA
     ALENKVENGT YRVADFSSRG YSWTDGDYAI QKGDVEISAP GAAIYSTWFD GGYATISGTS
     MASPHAAGLA AKIWAQYPSA SNVDVRGELQ YRAYENDILS GYYAGYGDDF ASGFGFATVQ