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 residuesNone
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.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP00782
UniProtKB Entry Name
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 ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
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 ]

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