| General information | | DisProt: | DP00394 | | Name: | Subtilisin E | | Synonym(s): | SUBT_BACSU
EC 3.4.21.62
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P04189 | | UniGene: | | | SwissProt: | SUBT_BACSU | | TrEMBL: | | | NCBI (GI): | 239938846 | | Source organism: | Bacillus subtilis | | Sequence length: | 381 | | Percent disordered: | 20% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM SSAKKKDVIS - 60
EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED HIAHEYAQSV PYGISQIKAP - 120
ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV RGGASFVPSE TNPYQDGSSH GTHVAGTIAA - 180
LNNSIGVLGV APSASLYAVK VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPTGSTA - 240
LKTVVDKAVS SGIVVAAAAG NEGSSGSTST VGYPAKYPST IAVGAVNSSN QRASFSSAGS - 300
ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTA - 360
TYLGNSFYYG KGLINVQAAA Q
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| Functional narrative |
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | pro-peptide | | Location: | 30 - 106 | | Length: | 77 | | Region sequence: |
AGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELK
KDPSVAYVEEDHIAHEY | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Chaperones
| | Functional subclasses: | Autoregulatory
| Detection methods:
- Nuclear magnetic resonance (NMR) (282 K; pH: 6; sodium phosphate (buffer) 50 mM)
| References:
- Buevich AV, Shinde UP, Inouye M, Baum J. "Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies." J Biomol NMR. 2001; 20(3): 233-49. PubMed: 11519747
| Comments:
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| References |
- Ikemura H, Takagi H, Inouye M. "Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli." J Biol Chem. 1987; 262(16): 7859-64. PubMed: 3108260
- Subbian E, Yabuta Y, Shinde UP. "Folding pathway mediated by an intramolecular chaperone: intrinsically unstructured propeptide modulates stochastic activation of subtilisin." J Mol Biol. 2005; 347(2): 367-83. PubMed: 15740747
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