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
- Functionsmetal ion binding / serine-type endopeptidase activityProcessessporulation 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.
- 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
Resource Link UniProtKB ID P00780 UniProtKB Entry Name SUBT_BACLI GenBank Protein ID 5921206 GenBank Gene ID X03341 - General References
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01942 Formic acid experimental, investigational unknown Details DB02560 [(1S)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boron experimental unknown Details DB02677 D-naphthyl-1-acetamido boronic acid alanine experimental unknown Details DB03290 L-naphthyl-1-acetamido boronic acid alanine experimental unknown Details DB03316 1,4-Dioxane experimental unknown Details DB03607 [(1R)-1-acetamido-2-(4-chlorophenyl)ethyl]-[(2S)-2-amino-3-hydroxy-3-oxo-propoxy]-dihydroxy-boron experimental unknown Details