SUBT_BACPU
ID SUBT_BACPU Reviewed; 275 AA.
AC P07518;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Subtilisin;
DE EC=3.4.21.62;
DE AltName: Full=Alkaline mesentericopeptidase;
GN Name=apr;
OS Bacillus pumilus (Bacillus mesentericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1408;
RN [1]
RP PROTEIN SEQUENCE.
RA Svendsen I., Genov N., Idakieva K.;
RT "Complete amino acid sequence of alkaline mesentericopeptidase: a
RT subtilisin isolated from a strain of Bacillus mesentericus.";
RL FEBS Lett. 196:228-232(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1793542; DOI=10.1107/s0108768191004202;
RA Dauter Z., Betzel C., Genov N., Pipon N., Wilson K.S.;
RT "Complex between the subtilisin from a mesophilic bacterium and the leech
RT inhibitor eglin-C.";
RL Acta Crystallogr. B 47:707-730(1991).
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;
CC Note=Binds 2 calcium ions per subunit.;
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 PIR; A23624; A23624.
DR PDB; 1MEE; X-ray; 2.00 A; A=1-275.
DR PDBsum; 1MEE; -.
DR AlphaFoldDB; P07518; -.
DR BMRB; P07518; -.
DR SMR; P07518; -.
DR MINT; P07518; -.
DR MEROPS; S08.002; -.
DR EvolutionaryTrace; P07518; -.
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; 3.40.50.200; -; 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; IPR034202; Subtilisin_Carlsberg-like.
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 3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Protease; Secreted; Serine protease; Sporulation.
FT CHAIN 1..275
FT /note="Subtilisin"
FT /id="PRO_0000076419"
FT DOMAIN 5..274
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 32
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 2
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1MEE"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1MEE"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1MEE"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:1MEE"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:1MEE"
SQ SEQUENCE 275 AA; 27656 MW; 33BDA897DBA4170A CRC64;
AQSVPYGISQ IKAPALHSQG YTGSNVKVAV IDSGIDSSHP DLNVRGGASF VPSETNPYQD
GSSHGTHVAG TIAALNNSIG VLGVAPSSAL YAVKVLDSTG SGQYSWIING IEWAISNNMD
VINMSLGGPT GSTALKTVVD KAVSSGIVVA AAAGNEGSSG STSTVGYPAK YPSTIAVGAV
NSANQRASFS SAGSELDVMA PGVSIQSTLP GGTYGAYNGT SMATPHVAGA AALILSKHPT
WTNAQVRDRL ESTATYLGSS FYYGKGLINV QAAAQ
