SUBB_LEDLE
ID SUBB_LEDLE Reviewed; 269 AA.
AC P29599;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Subtilisin BL;
DE EC=3.4.21.62;
DE AltName: Full=Alkaline protease;
OS Lederbergia lenta (Bacillus lentus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lederbergia.
OX NCBI_TaxID=1467;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=1453465; DOI=10.1016/0022-2836(92)90843-9;
RA Goddette D.W., Paech C., Yang S.S., Mielenz J.R., Bystroff C., Wilke M.E.,
RA Fletterick R.J.;
RT "The crystal structure of the Bacillus lentus alkaline protease, subtilisin
RT BL, at 1.4-A resolution.";
RL J. Mol. Biol. 228:580-595(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;
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; 1ST3; X-ray; 1.40 A; A=2-269.
DR PDBsum; 1ST3; -.
DR AlphaFoldDB; P29599; -.
DR SMR; P29599; -.
DR BindingDB; P29599; -.
DR ChEMBL; CHEMBL4258; -.
DR MEROPS; S08.003; -.
DR SABIO-RK; P29599; -.
DR EvolutionaryTrace; P29599; -.
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; Hydrolase; Metal-binding; Protease; Secreted;
KW Serine protease; Sporulation.
FT CHAIN 1..269
FT /note="Subtilisin BL"
FT /id="PRO_0000076416"
FT DOMAIN 5..268
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 62
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
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 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 73
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 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1ST3"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1ST3"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1ST3"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:1ST3"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1ST3"
SQ SEQUENCE 269 AA; 26824 MW; E8AFF1A6A9E2676B CRC64;
AQSVPWGISR VQAPAAHNRG LTGSGVKVAV LDTGISTHPD LNIRGGASFV PGEPSTQDGN
GHGTHVAGTI AALNNSIGVL GVAPSAELYA VKVLGADGRG AISSIAQGLE WAGNNGMHVA
NLSLGSPSPS ATLEQAVNSA TSRGVLVVAA SGNSGASSIS YPARYANAMA VGATDQNNNR
ASFSQYGAGL DIVAPGVNVQ STYPGSTYAS LNGTSMATPH VAGAAALVKQ KNPSWSNVQI
RNHLKNTATS LGSTNLYGSG LVNAEAATR
