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 02-SEP-2026, entry version 113. DE RecName: Full=Subtilisin BL; DE EC=3.4.21.62; DE AltName: Full=Alkaline protease; OS Lederbergia lenta (Bacillus lentus). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 1ST3; X-ray; 1.40 A; A=1-269. 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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; IPR050131; Peptidase_S8_subtilisin-like. DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel. DR InterPro; IPR034202; Subtilisin_Carlsberg-like. DR PANTHER; PTHR43806:SF11; CEREVISIN-RELATED; 1. DR PANTHER; PTHR43806; PEPTIDASE S8; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF52743; Subtilisin-like; 1. DR PROSITE; PS51892; SUBTILASE; 1. DR PROSITE; PS00136; SUBTILASE_ASP; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. DR PDBsum; 1ST3; -. 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 //