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Subtilisin BPN' (EC 3.4.21.62) (Alkaline protease) (Subtilisin DFE) (Subtilisin Novo)

 SUBT_BACAM              Reviewed;         382 AA.
P00782; P83945; Q44684;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=Subtilisin BPN';
EC=3.4.21.62;
AltName: Full=Alkaline protease;
AltName: Full=Subtilisin DFE;
AltName: Full=Subtilisin Novo;
Flags: Precursor;
Name=apr;
Bacillus amyloliquefaciens (Bacillus velezensis).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus amyloliquefaciens group.
NCBI_TaxID=1390;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 23844 / P;
PubMed=6090391;
Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J.,
Filpula D.;
"Genes for alkaline protease and neutral protease from Bacillus
amyloliquefaciens contain a large open reading frame between the
regions coding for signal sequence and mature protein.";
J. Bacteriol. 159:811-819(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-382.
PubMed=6316278; DOI=10.1093/nar/11.22.7911;
Wells J.A., Ferrari E., Henner D.J., Estell D.A., Chen E.Y.;
"Cloning, sequencing, and secretion of Bacillus amyloliquefaciens
subtilisin in Bacillus subtilis.";
Nucleic Acids Res. 11:7911-7925(1983).
[3]
PROTEIN SEQUENCE OF 108-382.
PubMed=6065094;
Markland F.S., Smith E.L.;
"Subtilisin BPN. VII. Isolation of cyanogen bromide peptides and the
complete amino acid sequence.";
J. Biol. Chem. 242:5198-5211(1967).
[4]
PROTEIN SEQUENCE OF 108-131, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND VARIANT PHE-128.
STRAIN=DC-4;
PubMed=12524032; DOI=10.1016/S1096-4959(02)00183-5;
Peng Y., Huang Q., Zhang R.-H., Zhang Y.-Z.;
"Purification and characterization of a fibrinolytic enzyme produced
by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional
Chinese soybean food.";
Comp. Biochem. Physiol. 134B:45-52(2003).
[5]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=4399039; DOI=10.1098/rstb.1970.0014;
Alden R.A., Wright C.S., Kraut J.;
"A hydrogen-bond network at the active site of subtilisin BPN'.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:119-124(1970).
[6]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
PubMed=6387152; DOI=10.1016/0022-2836(84)90150-5;
Hirono S., Akagawa H., Mitsui Y., Iitaka Y.;
"Crystal structure at 2.6-A resolution of the complex of subtilisin
BPN' with streptomyces subtilisin inhibitor.";
J. Mol. Biol. 178:389-413(1984).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
PubMed=2684274; DOI=10.1021/bi00444a012;
Pantoliano M.W., Whitlow M., Wood J.F., Dodd S.W., Hardman K.D.,
Rollence M.L., Bryan P.N.;
"Large increases in general stability for subtilisin BPN' through
incremental changes in the free energy of unfolding.";
Biochemistry 28:7205-7213(1989).
[8]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=15299573; DOI=10.1107/S0907444996007500;
Gallagher T., Oliver J., Bott R., Betzel C., Gilliland G.L.;
"Subtilisin BPN' at 1.6-A resolution: analysis for discrete disorder
and comparison of crystal forms.";
Acta Crystallogr. D 52:1125-1135(1996).
[9]
ACTIVE SITE.
PubMed=5249818; DOI=10.1073/pnas.61.4.1440;
Markland F.S., Shaw E., Smith E.L.;
"Identification of histidine 64 in the active site of subtilisin.";
Proc. Natl. Acad. Sci. U.S.A. 61:1440-1447(1968).
-!- FUNCTION: Subtilisin is an extracellular alkaline serine protease,
it catalyzes the hydrolysis of proteins and peptide amides. Has a
high substrate specificity to fibrin.
{ECO:0000269|PubMed:12524032}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity
for peptide bonds, and a preference for a large uncharged residue
in P1. Hydrolyzes peptide amides.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- ENZYME REGULATION: Completely inhibited by phenylmethylsulfony
fluoride (PMSF) and partially inhibited by benzamidine
hydrochloride, leupeptin, and pepstatin A.
{ECO:0000269|PubMed:12524032}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 9.0. {ECO:0000269|PubMed:12524032};
Temperature dependence:
Optimum temperature is 48 degrees Celsius.
{ECO:0000269|PubMed:12524032};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12524032}.
-!- INTERACTION:
Q40059:Ica-2 (xeno); NbExp=8; IntAct=EBI-1033955, EBI-1040468;
-!- SUBCELLULAR LOCATION: Secreted.
-!- BIOTECHNOLOGY: Used as a detergent protease. Sold under the name
Alcalase by Novozymes.
-!- MISCELLANEOUS: Secretion of subtilisin is associated with onset of
sporulation, and many mutations which block sporulation at early
stages affect expression levels of subtilisin. However, subtilisin
is not necessary for normal sporulation.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA24990.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K02496; AAB05345.1; -; Genomic_DNA.
EMBL; X00165; CAA24990.1; ALT_INIT; Genomic_DNA.
PIR; B25415; SUBSN.
RefSeq; WP_013351733.1; NZ_MOEA01000001.1.
PDB; 1A2Q; X-ray; 1.80 A; A=108-382.
PDB; 1AK9; X-ray; 1.80 A; A=108-382.
PDB; 1AQN; X-ray; 1.80 A; A=108-382.
PDB; 1AU9; X-ray; 1.80 A; A=108-382.
PDB; 1DUI; X-ray; 2.00 A; A=108-382.
PDB; 1GNS; X-ray; 1.80 A; A=112-382.
PDB; 1GNV; X-ray; 1.90 A; A=108-382.
PDB; 1LW6; X-ray; 1.50 A; E=108-382.
PDB; 1S01; X-ray; 1.70 A; A=108-382.
PDB; 1S02; X-ray; 1.90 A; A=108-382.
PDB; 1SBH; X-ray; 1.80 A; A=108-382.
PDB; 1SBI; X-ray; 2.20 A; A=108-382.
PDB; 1SBN; X-ray; 2.10 A; E=108-382.
PDB; 1SBT; X-ray; 2.50 A; A=108-382.
PDB; 1SIB; X-ray; 2.40 A; E=108-382.
PDB; 1SPB; X-ray; 2.00 A; P=37-107, S=108-382.
PDB; 1ST2; X-ray; 2.00 A; A=108-382.
PDB; 1SUA; X-ray; 2.10 A; A=108-382.
PDB; 1SUB; X-ray; 1.75 A; A=108-382.
PDB; 1SUC; X-ray; 1.80 A; A=108-382.
PDB; 1SUD; X-ray; 1.90 A; A=108-382.
PDB; 1SUE; X-ray; 1.80 A; A=108-382.
PDB; 1SUP; X-ray; 1.60 A; A=108-382.
PDB; 1TM1; X-ray; 1.70 A; E=108-382.
PDB; 1TM3; X-ray; 1.57 A; E=108-382.
PDB; 1TM4; X-ray; 1.70 A; E=108-382.
PDB; 1TM5; X-ray; 1.45 A; E=108-382.
PDB; 1TM7; X-ray; 1.59 A; E=108-382.
PDB; 1TMG; X-ray; 1.67 A; E=108-382.
PDB; 1TO1; X-ray; 1.68 A; E=108-382.
PDB; 1TO2; X-ray; 1.30 A; E=108-382.
PDB; 1UBN; X-ray; 2.40 A; A=108-382.
PDB; 1V5I; X-ray; 1.50 A; A=108-382.
PDB; 1Y1K; X-ray; 1.56 A; E=108-382.
PDB; 1Y33; X-ray; 1.80 A; E=108-382.
PDB; 1Y34; X-ray; 1.55 A; E=108-382.
PDB; 1Y3B; X-ray; 1.80 A; E=108-382.
PDB; 1Y3C; X-ray; 1.69 A; E=108-382.
PDB; 1Y3D; X-ray; 1.80 A; E=108-382.
PDB; 1Y3F; X-ray; 1.72 A; E=108-382.
PDB; 1Y48; X-ray; 1.84 A; E=108-382.
PDB; 1Y4A; X-ray; 1.60 A; E=108-382.
PDB; 1Y4D; X-ray; 2.00 A; E=108-382.
PDB; 1YJA; X-ray; 1.80 A; A=108-382.
PDB; 1YJB; X-ray; 1.80 A; A=108-382.
PDB; 1YJC; X-ray; 1.80 A; A=108-382.
PDB; 2SBT; X-ray; 2.80 A; A=108-382.
PDB; 2SIC; X-ray; 1.80 A; E=108-382.
PDB; 2SNI; X-ray; 2.10 A; E=108-382.
PDB; 2ST1; X-ray; 1.80 A; A=108-382.
PDB; 3BGO; X-ray; 1.80 A; P=32-111, S=108-382.
PDB; 3CNQ; X-ray; 1.71 A; P=32-111, S=108-382.
PDB; 3CO0; X-ray; 1.93 A; P=32-111, S=108-382.
PDB; 3F49; X-ray; 1.70 A; S=108-382.
PDB; 3SIC; X-ray; 1.80 A; E=108-382.
PDB; 5SIC; X-ray; 2.20 A; E=108-382.
PDBsum; 1A2Q; -.
PDBsum; 1AK9; -.
PDBsum; 1AQN; -.
PDBsum; 1AU9; -.
PDBsum; 1DUI; -.
PDBsum; 1GNS; -.
PDBsum; 1GNV; -.
PDBsum; 1LW6; -.
PDBsum; 1S01; -.
PDBsum; 1S02; -.
PDBsum; 1SBH; -.
PDBsum; 1SBI; -.
PDBsum; 1SBN; -.
PDBsum; 1SBT; -.
PDBsum; 1SIB; -.
PDBsum; 1SPB; -.
PDBsum; 1ST2; -.
PDBsum; 1SUA; -.
PDBsum; 1SUB; -.
PDBsum; 1SUC; -.
PDBsum; 1SUD; -.
PDBsum; 1SUE; -.
PDBsum; 1SUP; -.
PDBsum; 1TM1; -.
PDBsum; 1TM3; -.
PDBsum; 1TM4; -.
PDBsum; 1TM5; -.
PDBsum; 1TM7; -.
PDBsum; 1TMG; -.
PDBsum; 1TO1; -.
PDBsum; 1TO2; -.
PDBsum; 1UBN; -.
PDBsum; 1V5I; -.
PDBsum; 1Y1K; -.
PDBsum; 1Y33; -.
PDBsum; 1Y34; -.
PDBsum; 1Y3B; -.
PDBsum; 1Y3C; -.
PDBsum; 1Y3D; -.
PDBsum; 1Y3F; -.
PDBsum; 1Y48; -.
PDBsum; 1Y4A; -.
PDBsum; 1Y4D; -.
PDBsum; 1YJA; -.
PDBsum; 1YJB; -.
PDBsum; 1YJC; -.
PDBsum; 2SBT; -.
PDBsum; 2SIC; -.
PDBsum; 2SNI; -.
PDBsum; 2ST1; -.
PDBsum; 3BGO; -.
PDBsum; 3CNQ; -.
PDBsum; 3CO0; -.
PDBsum; 3F49; -.
PDBsum; 3SIC; -.
PDBsum; 5SIC; -.
ProteinModelPortal; P00782; -.
SMR; P00782; -.
IntAct; P00782; 2.
MINT; MINT-242921; -.
DrugBank; DB03297; Benzylsulfinic Acid.
DrugBank; DB04491; Diisopropylphosphono Group.
DrugBank; DB02442; Dioxyselenocysteine.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB01805; Monoisopropylphosphorylserine.
DrugBank; DB01915; S-Hydroxycysteine.
MEROPS; I09.001; -.
GeneID; 9780852; -.
eggNOG; COG1404; LUCA.
BRENDA; 3.4.21.62; 630.
SABIO-RK; P00782; -.
EvolutionaryTrace; P00782; -.
PMAP-CutDB; P00782; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
CDD; cd07477; Peptidases_S8_Subtilisin_subse; 1.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR010259; S8pro/Inhibitor_I9.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
InterPro; IPR034202; Subtilisin_Carlsberg-like.
Pfam; PF05922; Inhibitor_I9; 1.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Hydrolase;
Metal-binding; Protease; Secreted; Serine protease; Signal;
Sporulation; Zymogen.
SIGNAL 1 30 {ECO:0000250}.
PROPEP 31 107 {ECO:0000269|PubMed:12524032,
ECO:0000269|PubMed:6065094}.
/FTId=PRO_0000027177.
CHAIN 108 382 Subtilisin BPN'.
/FTId=PRO_0000027178.
DOMAIN 134 380 Peptidase S8.
ACT_SITE 139 139 Charge relay system.
{ECO:0000269|PubMed:5249818}.
ACT_SITE 171 171 Charge relay system.
{ECO:0000269|PubMed:5249818}.
ACT_SITE 328 328 Charge relay system.
{ECO:0000269|PubMed:5249818}.
METAL 109 109 Calcium 1.
METAL 148 148 Calcium 1.
METAL 182 182 Calcium 1; via carbonyl oxygen.
METAL 184 184 Calcium 1.
METAL 186 186 Calcium 1; via carbonyl oxygen.
METAL 188 188 Calcium 1; via carbonyl oxygen.
METAL 276 276 Calcium 2; via carbonyl oxygen.
METAL 278 278 Calcium 2; via carbonyl oxygen.
METAL 281 281 Calcium 2; via carbonyl oxygen.
VARIANT 128 128 Y -> F (in strain: DC-4).
{ECO:0000269|PubMed:12524032}.
STRAND 39 44 {ECO:0000244|PDB:3CNQ}.
TURN 46 49 {ECO:0000244|PDB:1SPB}.
HELIX 53 61 {ECO:0000244|PDB:3CNQ}.
TURN 62 64 {ECO:0000244|PDB:3CNQ}.
STRAND 66 70 {ECO:0000244|PDB:3CNQ}.
STRAND 72 80 {ECO:0000244|PDB:3CNQ}.
HELIX 83 90 {ECO:0000244|PDB:3CNQ}.
STRAND 95 100 {ECO:0000244|PDB:3CNQ}.
STRAND 103 106 {ECO:0000244|PDB:3CNQ}.
HELIX 113 117 {ECO:0000244|PDB:1TO2}.
HELIX 120 126 {ECO:0000244|PDB:1TO2}.
STRAND 134 140 {ECO:0000244|PDB:1TO2}.
STRAND 146 148 {ECO:0000244|PDB:1SUA}.
STRAND 151 156 {ECO:0000244|PDB:1TO2}.
STRAND 158 160 {ECO:0000244|PDB:2SBT}.
STRAND 168 170 {ECO:0000244|PDB:1TO2}.
HELIX 171 180 {ECO:0000244|PDB:1TO2}.
STRAND 183 188 {ECO:0000244|PDB:1TO2}.
HELIX 189 191 {ECO:0000244|PDB:3CNQ}.
STRAND 195 201 {ECO:0000244|PDB:1TO2}.
STRAND 207 209 {ECO:0000244|PDB:1TO2}.
HELIX 211 223 {ECO:0000244|PDB:1TO2}.
STRAND 227 231 {ECO:0000244|PDB:1TO2}.
STRAND 233 236 {ECO:0000244|PDB:1TO2}.
HELIX 240 251 {ECO:0000244|PDB:1TO2}.
STRAND 255 259 {ECO:0000244|PDB:1TO2}.
TURN 275 277 {ECO:0000244|PDB:1TO2}.
STRAND 281 287 {ECO:0000244|PDB:1TO2}.
STRAND 289 291 {ECO:0000244|PDB:2SBT}.
STRAND 305 308 {ECO:0000244|PDB:1TO2}.
STRAND 310 316 {ECO:0000244|PDB:1TO2}.
TURN 317 319 {ECO:0000244|PDB:1TO2}.
STRAND 320 324 {ECO:0000244|PDB:1TO2}.
HELIX 327 344 {ECO:0000244|PDB:1TO2}.
HELIX 350 358 {ECO:0000244|PDB:1TO2}.
STRAND 360 362 {ECO:0000244|PDB:1SPB}.
HELIX 367 370 {ECO:0000244|PDB:1TO2}.
HELIX 377 380 {ECO:0000244|PDB:1TO2}.
SEQUENCE 382 AA; 39181 MW; ED987DAFA37B8335 CRC64;
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST MSAAKKKDVI
SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE DHVAHAYAQS VPYGVSQIKA
PALHSQGYTG SNVKVAVIDS GIDSSHPDLK VAGGASMVPS ETNPFQDNNS HGTHVAGTVA
ALNNSIGVLG VAPSASLYAV KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA
ALKAAVDKAV ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN TQVRSSLENT
TTKLGDSFYY GKGLINVQAA AQ


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