Subtilisin Carlsberg

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	None
Molecular Weight	38907.64
Theoretical pI	9.19
GO Classification	Functions serine-type endopeptidase activity metal ion binding 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P00780
UniProtKB Entry Name
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
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. [3001653 ] 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. [4967581 ] 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. [8512925 ] 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. [9425066 ]

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