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[1]
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X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
DOI=10.1016/0022-2836(92)90843-9; PubMed=1453465 [NCBI, ExPASy, EBI, Israel, Japan]
Goddette D.W.,
Paech C.,
Yang S.S.,
Mielenz J.R.,
Bystroff C.,
Wilke M.E.,
Fletterick R.J.;
"The crystal structure of the Bacillus lentus alkaline protease, subtilisin BL, at 1.4-A resolution.";
J. Mol. Biol. 228:580-595(1992).
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- FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
- COFACTOR: Binds 2 calcium ions per subunit.
- SUBCELLULAR LOCATION: Secreted.
- MISCELLANEOUS: Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.
- SIMILARITY: Belongs to the peptidase S8 family [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 269 AA [This is the length of the unprocessed precursor] |
Molecular weight: 26824 Da [This is the MW of the unprocessed precursor] |
CRC64: E8AFF1A6A9E2676B [This is a checksum on the sequence] |
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10 20 30 40 50 60
AQSVPWGISR VQAPAAHNRG LTGSGVKVAV LDTGISTHPD LNIRGGASFV PGEPSTQDGN
70 80 90 100 110 120
GHGTHVAGTI AALNNSIGVL GVAPSAELYA VKVLGADGRG AISSIAQGLE WAGNNGMHVA
130 140 150 160 170 180
NLSLGSPSPS ATLEQAVNSA TSRGVLVVAA SGNSGASSIS YPARYANAMA VGATDQNNNR
190 200 210 220 230 240
ASFSQYGAGL DIVAPGVNVQ STYPGSTYAS LNGTSMATPH VAGAAALVKQ KNPSWSNVQI
250 260
RNHLKNTATS LGSTNLYGSG LVNAEAATR
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P29599 in FASTA format |
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