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MYP_108173
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Basic Information
ydhT signal peptide
Annotation / Sequence feature ▸ Signal peptide
Biotechnology / Production and expression ▸ Secretory expression optimization
Enzyme / Catalytic activity ▸ Protease ▸ Bacillus protease novo type (BPN') secretion
Enzyme / Catalytic activity ▸ Transferase ▸ Kinase
Standard
24 amino acids
C122H196N28O31S2
Standard
Sequence
MKKNIVCSIFALLLAFAVSQPSYA
Physicochemical Analysis
2615.16 Da
9.19
1.49
1.25
0.0620
1.08
0.42
0.38
58.30
122.08
0.1250
1490.00
1490.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
942.97
-5.83
33.0
35.0
84.0
183.0
4.0
25.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0171647 VERIFIED: YES
Provenance & Taxonomy
Bacillus licheniformis DSM 13 = ATCC 14580 [Bacterium]
Sec signal peptide
279010
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Bacillus protease novo type (BPN') secretion
Bacillus subtilis TEB1030
3.38 U/mL
Protease activity assay
PaperDegering C, Eggert T, Puls M, et al. Optimization of Protease Secretion in Bacillus subtilis and Bacillus licheniformis by Screening of Homologous and Heterologous Signal Peptides[J]. Applied and Environmental Microbiology, 2010, 76(19): 6370-6376. PMID20709850 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20709850/
RECORD: Rec_0298221 VERIFIED: YES
Provenance & Taxonomy
Bacillus licheniformis DSM 13 = ATCC 14580 [Bacterium]
Sec signal peptide
279010
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Bacillus protease novo type (BPN') secretion
Bacillus licheniformis △0F-3
1.41 U/mL
Protease activity assay
PaperDegering C, Eggert T, Puls M, et al. Optimization of Protease Secretion in Bacillus subtilis and Bacillus licheniformis by Screening of Homologous and Heterologous Signal Peptides[J]. Applied and Environmental Microbiology, 2010, 76(19): 6370-6376. PMID20709850 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20709850/
RECORD: Rec_0349866 VERIFIED: YES
Provenance & Taxonomy
Bacillus licheniformis WX-02 [Bacterium]
Sec signal peptide
1126218
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Nattokinase secretion
Bacillus licheniformis △0F-3
11.01 FU/mL
Fibrinolytic activity assay
PaperCai D, Wei X, Qiu Y, et al. High-level expression of nattokinase in Bacillus licheniformis by manipulating signal peptide and signal peptidase[J]. Journal of Applied Microbiology, 2016, 121(3): 704-712. PMID27159567 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27159567/
RECORD: Rec_0407432 VERIFIED: YES
Provenance & Taxonomy
Bacillus licheniformis DSM 13 = ATCC 14580 [Bacterium]
Sec signal peptide
279010
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Bacillus protease novo type (BPN') secretion
Bacillus licheniformis △0F-3
1.19 U/mL
Protease activity assay
PaperDegering C, Eggert T, Puls M, et al. Optimization of Protease Secretion in Bacillus subtilis and Bacillus licheniformis by Screening of Homologous and Heterologous Signal Peptides[J]. Applied and Environmental Microbiology, 2010, 76(19): 6370-6376. PMID20709850 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20709850/