Subtilisin BPN'

NameSubtilisin BPN'
Synonyms
  • 3.4.21.62
  • Alkaline protease
  • Subtilisin DFE
  • Subtilisin Novo
Gene Nameapr
OrganismBacillus amyloliquefaciens
Amino acid sequence
>lcl|BSEQ0002733|Subtilisin BPN'
MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVI
SEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKA
PALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVA
ALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSA
ALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVG
PELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENT
TTKLGDSFYYGKGLINVQAAAQ
Number of residues382
Molecular Weight39180.935
Theoretical pI9.61
GO Classification
Functions
  • serine-type endopeptidase activity
  • metal ion binding
Processes
  • proteolysis
  • fibrinolysis
  • sporulation resulting in formation of a cellular spore
Components
  • extracellular region
General FunctionSerine-type endopeptidase activity
Specific FunctionSubtilisin 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 RegionsNot Available
GenBank Protein ID142526
UniProtKB IDP00782
UniProtKB Entry NameSUBT_BACAM
Cellular LocationSecreted
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
GenBank Gene IDK02496
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. 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. 6090391
  2. 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. 6316278
  3. 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. 6065094
  4. 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. 12524032
  5. 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. 4399039
  6. 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. 6387152
  7. 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. 2684274
  8. 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. 15299573
  9. 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. 5249818