SUBD_BACLI
ID SUBD_BACLI Reviewed; 274 AA.
AC P00781;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Subtilisin DY;
DE EC=3.4.21.62;
GN Name=apr;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=DY;
RX PubMed=6420308; DOI=10.1515/bchm2.1983.364.2.1537;
RA Nedkov P., Oberthur W., Braunitzer G.;
RT "Primary structure of subtilisin DY.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1537-1540(1983).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RC STRAIN=DY;
RX PubMed=9826175; DOI=10.1046/j.1432-1327.1998.2570309.x;
RA Eschenburg S., Genov N., Peters K., Fittkau S., Stoeva S., Wilson K.S.,
RA Betzel C.;
RT "Crystal structure of subtilisin DY, a random mutant of subtilisin
RT Carlsberg.";
RL Eur. J. Biochem. 257:309-318(1998).
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 PDB; 1BH6; X-ray; 1.75 A; A=1-274.
DR PDBsum; 1BH6; -.
DR AlphaFoldDB; P00781; -.
DR SMR; P00781; -.
DR DrugBank; DB06886; N-BENZYLOXYCARBONYL-ALA-PRO-3-AMINO-4-PHENYL-BUTAN-2-OL.
DR MEROPS; S08.037; -.
DR EvolutionaryTrace; P00781; -.
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..274
FT /note="Subtilisin DY"
FT /id="PRO_0000076417"
FT DOMAIN 5..273
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 63
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 220
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 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1BH6"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:1BH6"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1BH6"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 219..236
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1BH6"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1BH6"
SQ SEQUENCE 274 AA; 27436 MW; 0154696E22F46533 CRC64;
AQTVPYGIPL IKADKVQAQG YKGANVKVGI IDTGIAASHT DLKVVGGASF VSGESYNTDG
NGHGTHVAGT VAALDNTTGV LGVAPNVSLY AIKVLNSSGS GTYSAIVSGI EWATQNGLDV
INMSLGGPSG STALKQAVDK AYASGIVVVA AAGNSGSSGS QNTIGYPAKY DSVIAVGAVD
SNKNRASFSS VGAELEVMAP GVSVYSTYPS NTYTSLNGTS MASPHVAGAA ALILSKYPTL
SASQVRNRLS STATNLGDSF YYGKGLINVE AAAQ
