Subtilisin Carlsberg

Details

Name
Subtilisin Carlsberg
Synonyms
  • 3.4.21.62
Gene Name
apr
Organism
Bacillus licheniformis
Amino acid sequence
>lcl|BSEQ0016415|Subtilisin Carlsberg
MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKE
SGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADK
VQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALD
NTTGVLGVAPSVSLYAVKVLNSSGSGTYSGIVSGIEWATTNGMDVINMSLGGPSGSTAMK
QAVDNAYARGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAEL
EVMAPGAGVYSTYPTSTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATY
LGSSFYYGKGLINVEAAAQ
Number of residues
379
Molecular Weight
38907.64
Theoretical pI
9.19
GO Classification
Functions
metal ion binding / serine-type endopeptidase activity
Processes
sporulation resulting in formation of a cellular spore
Components
extracellular 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0002772|1140 bp
ATGATGAGGAAAAAGAGTTTTTGGCTTGGGATGCTGACGGCCTTCATGCTCGTGTTCACG
ATGGCATTCAGCGATTCCGCTTCTGCTGCTCAACCGGCGAAAAATGTTGAAAAGGATTAT
ATTGTCGGATTTAAGTCAGGAGTGAAAACCGCATCTGTCAAAAAGGACATCATCAAAGAG
AGCGGCGGAAAAGTGGACAAGCAGTTTAGAATCATCAACGCGGCAAAAGCGAAGCTAGAC
AAAGAAGCGCTTAAGGAAGTCAAAAATGATCCGGATGTCGCTTATGTGGAAGAGGATCAT
GTGGCCCATGCCTTGGCGCAAACCGTTCCTTACGGCATTCCTCTCATTAAAGCGGACAAA
GTGCAGGCTCAAGGCTTTAAGGGAGCGAATGTAAAAGTAGCCGTCCTGGATACAGGAATC
CAAGCTTCTCATCCGGACTTGAACGTAGTCGGCGGAGCAAGCTTTGTGGCTGGCGAAGCT
TATAACACCGACGGCAACGGACACGGCACACATGTTGCCGGTACAGTAGCTGCGCTTGAC
AATACAACGGGTGTATTAGGCGTTGCGCCAAGCGTATCCTTGTACGCGGTTAAAGTACTG
AATTCAAGCGGAAGCGGAACTTACAGCGGCATTGTAAGCGGAATCGAGTGGGCGACGACA
AACGGCATGGATGTTATCAACATGAGTCTTGGAGGACCATCAGGCTCAACAGCGATGAAA
CAGGCGGTTGACAATGCATATGCAAGAGGGGTTGTCGTTGTGGCGGCTGCTGGGAACAGC
GGATCTTCAGGAAACACGAATACAATCGGCTATCCTGCGAAATACGACTCTGTCATCGCA
GTTGGCGCGGTAGACTCTAACAGCAACAGAGCTTCATTTTCCAGCGTCGGAGCAGAGCTT
GAAGTCATGGCTCCTGGCGCAGGCGTGTACAGCACTTACCCAACCAGCACTTATGCAACA
TTGAACGGAACGTCAATGGCTTCTCCTCATGTAGCGGGAGCAGCAGCTTTGATCTTGTCA
AAACATCCGAACCTTTCAGCTTCACAAGTCCGCAACCGTCTCTCCAGTACGGCGACTTAT
TTGGGAAGCTCCTTCTACTATGGAAAAGGTCTGATCAATGTCGAAGCTGCCGCTCAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00780
UniProtKB Entry NameSUBT_BACLI
GenBank Protein ID5921206
GenBank Gene IDX03341
General References
  1. Jacobs M, Eliasson M, Uhlen M, Flock JI: Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis. Nucleic Acids Res. 1985 Dec 20;13(24):8913-26. [Article]
  2. Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS: Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. J Biol Chem. 1968 May 10;243(9):2184-91. [Article]
  3. Syed R, Wu ZP, Hogle JM, Hilvert D: Crystal structure of selenosubtilisin at 2.0-A resolution. Biochemistry. 1993 Jun 22;32(24):6157-64. [Article]
  4. Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF: Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes. Biochemistry. 1998 Jan 13;37(2):451-62. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01942Formic acidexperimental, investigationalunknownDetails
DB02560[(1S)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boronexperimentalunknownDetails
DB02677D-naphthyl-1-acetamido boronic acid alanineexperimentalunknownDetails
DB03290L-naphthyl-1-acetamido boronic acid alanineexperimentalunknownDetails
DB033161,4-DioxaneexperimentalunknownDetails
DB03607[(1R)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boronexperimentalunknownDetails