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MYP_138421
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Basic Information
ykoj signal peptide
Annotation / Sequence feature ▸ Signal peptide
Biotechnology / Production and expression ▸ Secretory enzyme production ▸ Alkaline protease secretion
Biotechnology / Production and expression ▸ Secretory enzyme production ▸ Cutinase secretion
Biotechnology / Production and expression ▸ Secretory expression optimization
Enzyme / Catalytic activity ▸ Hydrolase ▸ Glycosidase ▸ Xylanase
Enzyme modulation ▸ Enzyme inhibition ▸ Amylase inhibition ▸ Alpha-amylase inhibitory
Standard
26 amino acids
C128H199N31O30S3
Standard
Sequence
MLKKKWMVGLLAGCLAAGGFSYNAFA
Physicochemical Analysis
2748.33 Da
9.63
2.49
2.25
0.0956
0.79
0.23
0.38
24.35
90.38
0.1538
6990.00
6990.00
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
968.22
-5.17
35.0
36.0
90.0
192.0
5.0
26.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0041956 VERIFIED: YES
Provenance & Taxonomy
Bacillus subtilis [Bacterium]
Sec signal peptide
1423
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization alpha-amylase (AmyS) secretion
Bacillus subtilis 1A751
789.3 U/mL
Amylase activity assay
PaperJinlan L, Gang F, Huina D, et al. Optimization of thermostable alpha-amylase secretion by screening of optimal singal peptides in Bacillus subtilis[J]. Industrial Microbiology, 2017, 47(01): 17-23. (In Chinese)
RECORD: Rec_0073020 VERIFIED: YES
Provenance & Taxonomy
Bacillus subtilis [Bacterium]
Sec signal peptide
1423
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Alkaline active xylanase (XynBYG) secretion
Bacillus subtilis WB700
112.0 U/mL
Xylanase activity assay
PaperZhang W, Yang M, Yang Y, et al. Optimal secretion of alkali-tolerant xylanase in Bacillus subtilis by signal peptide screening[J]. Applied Microbiology and Biotechnology, 2016, 100(20): 8745-8756 PMID27225471 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27225471/
RECORD: Rec_0145370 VERIFIED: YES
Provenance & Taxonomy
Bacillus subtilis [Bacterium]
Sec signal peptide
1423
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Alkaline active xylanase (XynBYG) secretion
Bacillus subtilis WB700
67.2 U/mL
Xylanase activity assay
PaperZhang W, Yang M, Yang Y, et al. Optimal secretion of alkali-tolerant xylanase in Bacillus subtilis by signal peptide screening[J]. Applied Microbiology and Biotechnology, 2016, 100(20): 8745-8756 PMID27225471 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27225471/
RECORD: Rec_0326711 VERIFIED: YES
Provenance & Taxonomy
Bacillus subtilis subsp. subtilis str. 168 [Bacterium]
Sec signal peptide
224308
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Alkalineprotease (alk) secretion
Bacillus amyloliquefaciens 111018
10817.3 U/mL
Protease activity assay
PaperLiu Y, Shi C, Li D, et al. Engineering a highly efficient expression system to produce BcaPRO protease in Bacillus subtilis by an optimized promoter and signal peptide[J]. International journal of biological macromolecules, 2019, 138: 903-911. PMID31356949 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/31356949/
RECORD: Rec_0333881 VERIFIED: YES
Provenance & Taxonomy
Bacillus subtilis [Bacterium]
Sec signal peptide
1423
Structure & Mods
linear signal peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Protein secretion signal peptide Secretory expression optimization Alkalineprotease (alk) secretion
Bacillus amyloliquefaciens 111018
12078.78 U/mL
Protease activity assay
PaperLiu Y, Shi C, Li D, et al. Engineering a highly efficient expression system to produce BcaPRO protease in Bacillus subtilis by an optimized promoter and signal peptide[J]. International journal of biological macromolecules, 2019, 138: 903-911. PMID31356949 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/31356949/
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