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UniProtKB/Swiss-Prot entry P00782


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SUBT_BACAM
Primary accession number P00782
Secondary accession numbers P83945 Q44684
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 89)
Name and origin of the protein
Protein name Subtilisin BPN' [Precursor]
Synonyms EC 3.4.21.62
Subtilisin Novo
Subtilisin DFE
Alkaline protease
Gene name
Name: apr
From
Bacillus amyloliquefaciens [TaxID: 1390] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 23844 / P;
PubMed=6090391 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1093/nar/11.22.7911; PubMed=6316278 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1016/S1096-4959(02)00183-5; PubMed=12524032 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0022-2836(84)90150-5; PubMed=6387152 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1021/bi00444a012; PubMed=2684274 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1107/S0907444996007500; PubMed=15299573 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02496; AAB05345.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00165; CAA24990.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B25415; SUBSN.
3D structure databases
PDB
1A2Q; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1AK9; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1AQN; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1AU9; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1DUI; X-ray; 2.00 A; A=108-382.[ExPASy / RCSB / EBI]
1GNS; X-ray; 1.80 A; A=112-382.[ExPASy / RCSB / EBI]
1GNV; X-ray; 1.90 A; A=108-382.[ExPASy / RCSB / EBI]
1LW6; X-ray; 1.50 A; E=108-382.[ExPASy / RCSB / EBI]
1S01; X-ray; 1.70 A; A=108-382.[ExPASy / RCSB / EBI]
1S02; X-ray; 1.90 A; A=108-382.[ExPASy / RCSB / EBI]
1SBH; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1SBI; X-ray; 2.20 A; A=108-382.[ExPASy / RCSB / EBI]
1SBN; X-ray; 2.10 A; E=108-382.[ExPASy / RCSB / EBI]
1SBT; X-ray; 2.50 A; A=108-382.[ExPASy / RCSB / EBI]
1SIB; X-ray; 2.40 A; E=108-382.[ExPASy / RCSB / EBI]
1SPB; X-ray; 2.00 A; P=37-107, S=108-382.[ExPASy / RCSB / EBI]
1ST2; X-ray; 2.00 A; A=108-382.[ExPASy / RCSB / EBI]
1SUA; X-ray; 2.10 A; A=108-382.[ExPASy / RCSB / EBI]
1SUB; X-ray; 1.75 A; A=108-382.[ExPASy / RCSB / EBI]
1SUC; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1SUD; X-ray; 1.90 A; A=108-382.[ExPASy / RCSB / EBI]
1SUE; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1SUP; X-ray; 1.60 A; A=108-382.[ExPASy / RCSB / EBI]
1TM1; X-ray; 1.70 A; E=108-382.[ExPASy / RCSB / EBI]
1TM3; X-ray; 1.57 A; E=108-382.[ExPASy / RCSB / EBI]
1TM4; X-ray; 1.70 A; E=108-382.[ExPASy / RCSB / EBI]
1TM5; X-ray; 1.45 A; E=108-382.[ExPASy / RCSB / EBI]
1TM7; X-ray; 1.59 A; E=108-382.[ExPASy / RCSB / EBI]
1TMG; X-ray; 1.67 A; E=108-382.[ExPASy / RCSB / EBI]
1TO1; X-ray; 1.68 A; E=108-382.[ExPASy / RCSB / EBI]
1TO2; X-ray; 1.30 A; E=108-382.[ExPASy / RCSB / EBI]
1UBN; X-ray; 2.40 A; A=108-382.[ExPASy / RCSB / EBI]
1V5I; X-ray; 1.50 A; A=108-382.[ExPASy / RCSB / EBI]
1Y1K; X-ray; 1.56 A; E=108-382.[ExPASy / RCSB / EBI]
1Y33; X-ray; 1.80 A; E=108-382.[ExPASy / RCSB / EBI]
1Y34; X-ray; 1.55 A; E=108-382.[ExPASy / RCSB / EBI]
1Y3B; X-ray; 1.80 A; E=108-382.[ExPASy / RCSB / EBI]
1Y3C; X-ray; 1.69 A; E=108-382.[ExPASy / RCSB / EBI]
1Y3D; X-ray; 1.80 A; E=108-382.[ExPASy / RCSB / EBI]
1Y3F; X-ray; 1.72 A; E=108-382.[ExPASy / RCSB / EBI]
1Y48; X-ray; 1.84 A; E=108-382.[ExPASy / RCSB / EBI]
1Y4A; X-ray; 1.60 A; E=108-382.[ExPASy / RCSB / EBI]
1Y4D; X-ray; 2.00 A; E=108-382.[ExPASy / RCSB / EBI]
1YJA; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1YJB; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
1YJC; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
2SBT; X-ray; 2.80 A; A=108-382.[ExPASy / RCSB / EBI]
2SIC; X-ray; 1.80 A; E=108-382.[ExPASy / RCSB / EBI]
2SNI; X-ray; 2.10 A; E=108-382.[ExPASy / RCSB / EBI]
2ST1; X-ray; 1.80 A; A=108-382.[ExPASy / RCSB / EBI]
3SIC; X-ray; 1.80 A; E=108-382.[ExPASy / RCSB / EBI]
5SIC; X-ray; 2.20 A; E=108-382.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A2Q; -.
1AK9; -.
1AQN; -.
1AU9; -.
1DUI; -.
1GNS; -.
1GNV; -.
1LW6; -.
1S01; -.
1S02; -.
1SBH; -.
1SBI; -.
1SBN; -.
1SBT; -.
1SIB; -.
1SPB; -.
1ST2; -.
1SUA; -.
1SUB; -.
1SUC; -.
1SUD; -.
1SUE; -.
1SUP; -.
1TM1; -.
1TM3; -.
1TM4; -.
1TM5; -.
1TM7; -.
1TMG; -.
1TO1; -.
1TO2; -.
1UBN; -.
1V5I; -.
1Y1K; -.
1Y33; -.
1Y34; -.
1Y3B; -.
1Y3C; -.
1Y3D; -.
1Y3F; -.
1Y48; -.
1Y4A; -.
1Y4D; -.
1YJA; -.
1YJB; -.
1YJC; -.
2SBT; -.
2SIC; -.
2SNI; -.
2ST1; -.
3SIC; -.
5SIC; -.
ModBase P00782.
Protein-protein interaction databases
IntAct P00782; -.
Protein family/group databases
MEROPS I09.001; -.
S08.034; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from direct assay from UniProtKB).
GO:0042730; Biological process: fibrinolysis (inferred from direct assay from UniProtKB).
GO:0006508; Biological process: proteolysis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000209; Pept_S8_S53.
IPR015500; Peptidase_S8_subtilisin-rel.
IPR010259; Prot_inh_S8A.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.200; Pept_S8_S53; 1.
PANTHER PTHR10795; SubtilSerProt; 1.
Pfam PF00082; Peptidase_S8; 1.
PF05922; Subtilisin_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00723; SUBTILISIN.
PROSITE PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.
BLOCKS P00782.
ProtoNet P00782.
Other
LinkHub P00782; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Secreted; Serine protease; Signal; Sporulation; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    32  32     Potential. 
PROPEP   33   107  75      PRO_0000027177
CHAIN   108   382  275     Subtilisin BPN'. PRO_0000027178
ACT_SITE   139   139        Charge relay system. 
ACT_SITE   171   171        Charge relay system. 
ACT_SITE   328   328        Charge relay system. 
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  1     Y -> F (in strain: DC-4). 
STRAND   39    44  6      
TURN   46    49  4      
HELIX   53    62  10      
STRAND   66    70  5      
STRAND   72    80  9      
HELIX   83    91  9      
STRAND   95   100  6      
STRAND   103   106  4      
HELIX   113   117  5      
HELIX   120   126  7      
STRAND   134   140  7      
STRAND   151   156  6      
STRAND   168   170  3      
HELIX   171   180  10      
STRAND   183   188  6      
STRAND   196   201  6      
STRAND   207   209  3      
HELIX   211   223  13      
STRAND   227   231  5      
STRAND   233   236  4      
HELIX   240   251  12      
STRAND   255   259  5      
TURN   275   277  3      
STRAND   281   287  7      
STRAND   305   308  4      
STRAND   310   316  7      
TURN   317   319  3      
STRAND   320   324  5      
HELIX   327   344  18      
HELIX   350   358  9      
HELIX   367   370  4      
HELIX   377   380  4      
Sequence information
Length: 382 AA [This is the length of the unprocessed precursor] Molecular weight: 39181 Da [This is the MW of the unprocessed precursor] CRC64: ED987DAFA37B8335 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST MSAAKKKDVI 

        70         80         90        100        110        120 
SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE DHVAHAYAQS VPYGVSQIKA 

       130        140        150        160        170        180 
PALHSQGYTG SNVKVAVIDS GIDSSHPDLK VAGGASMVPS ETNPFQDNNS HGTHVAGTVA 

       190        200        210        220        230        240 
ALNNSIGVLG VAPSASLYAV KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA 

       250        260        270        280        290        300 
ALKAAVDKAV ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG 

       310        320        330        340        350        360 
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN TQVRSSLENT 

       370        380 
TTKLGDSFYY GKGLINVQAA AQ 

P00782 in FASTA format

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View entry in raw text format (no links)
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