Subtilisin BPN'
Details
- Name
- Subtilisin BPN'
- Synonyms
- 3.4.21.62
- Alkaline protease
- Subtilisin DFE
- Subtilisin Novo
- Gene Name
- apr
- Organism
- Bacillus amyloliquefaciens
- Amino acid sequence
>lcl|BSEQ0002733|Subtilisin BPN' MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVI SEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKA PALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVA ALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSA ALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVG PELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT TTKLGDSFYYGKGLINVQAAAQ
- Number of residues
- 382
- Molecular Weight
- 39180.935
- Theoretical pI
- 9.61
- GO Classification
- Functionsmetal ion binding / serine-type endopeptidase activityProcessesfibrinolysis / proteolysis / sporulation resulting in formation of a cellular sporeComponentsextracellular region
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0002732|1149 bp GTGAGAGGCAAAAAAGTATGGATCAGTTTGCTGTTTGCTTTAGCGTTAATCTTTACGATG GCGTTCGGCAGCACATCCTCTGCCCAGGCGGCAGGGAAATCAAACGGGGAAAAGAAATAT ATTGTCGGGTTTAAACAGACAATGAGCACGATGAGCGCCGCTAAGAAGAAAGATGTCATT TCTGAAAAAGGCGGGAAAGTGCAAAAGCAATTCAAATATGTAGACGCAGCTTCAGCTACA TTAAACGAAAAAGCTGTAAAAGAATTGAAAAAAGACCCGAGCGTCGCTTACGTTGAAGAA GATCACGTAGCACATGCGTACGCGCAGTCCGTGCCTTACGGCGTATCACAAATTAAAGCC CCTGCTCTGCACTCTCAAGGCTACACTGGATCAAATGTTAAAGTAGCGGTTATCGACAGC GGTATCGATTCTTCTCATCCTGATTTAAAGGTAGCAGGCGGAGCCAGCATGGTTCCTTCT GAAACAAATCCTTTCCAAGACAACAACTCTCACGGAACTCACGTTGCCGGCACAGTTGCG GCTCTTAATAACTCAATCGGTGTATTAGGCGTTGCGCCAAGCGCATCACTTTACGCTGTA AAAGTTCTCGGTGCTGACGGTTCCGGCCAATACAGCTGGATCATTAACGGAATCGAGTGG GCGATCGCAAACAATATGGACGTTATTAACATGAGCCTCGGCGGACCTTCTGGTTCTGCT GCTTTAAAAGCGGCAGTTGATAAAGCCGTTGCATCCGGCGTCGTAGTCGTTGCGGCAGCC GGTAACGAAGGCACTTCCGGCAGCTCAAGCACAGTGGGCTACCCTGGTAAATACCCTTCT GTCATTGCAGTAGGCGCTGTTGACAGCAGCAACCAAAGAGCATCTTTCTCAAGCGTAGGA CCTGAGCTTGATGTCATGGCACCTGGCGTATCTATCCAAAGCACGCTTCCTGGAAACAAA TACGGGGCGTACAACGGTACGTCAATGGCATCTCCGCACGTTGCCGGAGCGGCTGCTTTG ATTCTTTCTAAGCACCCGAACTGGACAAACACTCAAGTCCGCAGCAGTTTAGAAAACACC ACTACAAAACTTGGTGATTCTTTCTACTATGGAAAAGGGCTGATCAACGTACAGGCGGCA GCTCAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00782 UniProtKB Entry Name SUBT_BACAM GenBank Protein ID 142526 GenBank Gene ID K02496 - General References
- Vasantha N, Thompson LD, 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. 1984 Sep;159(3):811-9. [Article]
- Wells JA, Ferrari E, Henner DJ, Estell DA, Chen EY: Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis. Nucleic Acids Res. 1983 Nov 25;11(22):7911-25. [Article]
- Markland FS, Smith EL: Subtilisin BPN. VII. Isolation of cyanogen bromide peptides and the complete amino acid sequence. J Biol Chem. 1967 Nov 25;242(22):5198-211. [Article]
- Peng Y, Huang Q, Zhang RH, Zhang YZ: Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Physiol B Biochem Mol Biol. 2003 Jan;134(1):45-52. [Article]
- Alden RA, Wright CS, Kraut J: A hydrogen-bond network at the active site of subtilisin BPN'. Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):119-24. [Article]
- 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. 1984 Sep 15;178(2):389-414. [Article]
- Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN: Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Biochemistry. 1989 Sep 5;28(18):7205-13. [Article]
- Gallagher T, Oliver J, Bott R, Betzel C, Gilliland GL: Subtilisin BPN' at 1.6 A resolution: analysis for discrete disorder and comparison of crystal forms. Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1125-35. [Article]
- Markland FS, Shaw E, Smith EL: Identification of histidine 64 in the active site of subtilisin. Proc Natl Acad Sci U S A. 1968 Dec;61(4):1440-7. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01805 Monoisopropylphosphorylserine experimental unknown Details DB01915 S-Hydroxycysteine experimental unknown Details DB02442 Dioxyselenocysteine experimental unknown Details DB03297 Benzylsulfonic acid experimental unknown Details DB04491 Diisopropylphosphono Group experimental unknown Details