SUBT_BACSA
ID SUBT_BACSA Reviewed; 381 AA.
AC P00783;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Subtilisin amylosacchariticus;
DE EC=3.4.21.62;
DE Flags: Precursor;
GN Name=apr;
OS Bacillus subtilis subsp. amylosacchariticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3139650; DOI=10.1093/oxfordjournals.jbchem.a122380;
RA Yoshimoto T., Oyama H., Honda T., Tone H., Takeshita T., Kamiyama T.,
RA Tsuru D.;
RT "Cloning and expression of subtilisin amylosacchariticus gene.";
RL J. Biochem. 103:1060-1065(1988).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=4560201; DOI=10.1016/s0021-9258(20)81147-8;
RA Markland F.S., Kurihara M., Smith E.L.;
RT "Subtilisin Amylosacchariticus. II. Isolation and sequence of the tryptic
RT and cyanogen bromide peptides.";
RL J. Biol. Chem. 247:5602-5618(1972).
RN [3]
RP PROTEIN SEQUENCE OF 107-381.
RX PubMed=5055784; DOI=10.1016/s0021-9258(20)81148-x;
RA Kurihara M., Markland F.S., Smith E.L.;
RT "Subtilisin Amylosacchariticus. 3. Isolation and sequence of the
RT chymotryptic peptides and the complete amino acid sequence.";
RL J. Biol. Chem. 247:5619-5631(1972).
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:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
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; D00264; BAA00186.1; -; Genomic_DNA.
DR PIR; A41448; SUBSS.
DR AlphaFoldDB; P00783; -.
DR BMRB; P00783; -.
DR SMR; P00783; -.
DR MEROPS; S08.042; -.
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 CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 3.30.70.80; -; 1.
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 InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
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 Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease;
KW Secreted; Serine protease; Signal; Sporulation; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT PROPEP 30..106
FT /evidence="ECO:0000305|PubMed:5055784"
FT /id="PRO_0000027183"
FT CHAIN 107..381
FT /note="Subtilisin amylosacchariticus"
FT /id="PRO_0000027184"
FT DOMAIN 38..103
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 111..380
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 191
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 39467 MW; 2251BADE22B4824F CRC64;
MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM SSAKKKDVIS
EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED HIAHEYAQSV PYGISQIKAP
ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV RGGASFVPSE TNPYQDGSSH GTHVAGTIAA
LNNSIGVLGV SPSASLYAVK VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPSGSTA
LKTVVDKAVS SGIVVAAAAG NEGSSGSSST VGYPAKYPST IAVGAVNSSN QRASFSSAGS
ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTA
TYLGNSFYYG KGLINVQAAA Q
