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MYP_053670
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Basic Information
estB signal peptide
Annotation / Sequence feature ▸ Signal peptide
Biotechnology / Production and expression ▸ Secretory enzyme production ▸ Cutinase secretion
Biotechnology / Production and expression ▸ Secretory expression optimization
Enzyme / Catalytic activity ▸ Hydrolase ▸ Glycosidase ▸ Xylanase
Enzyme / Catalytic activity ▸ Hydrolase ▸ Lipase
Enzyme modulation ▸ Enzyme inhibition ▸ Amylase inhibition ▸ Alpha-amylase inhibitory
Standard
28 amino acids
C134H233N31O32S3
Standard
Sequence
MKKVLMAFIICLSLILSVLAAPPSGAKA
Physicochemical Analysis
2886.67 Da
9.79
2.49
2.25
0.0888
1.48
0.30
0.47
42.38
150.00
0.0357
0.00
0.00
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
970.19
-4.05
34.0
38.0
95.0
200.0
3.0
27.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0032674 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 Cutinase secretion
Bacillus subtilis TEB1030
1.62 U/mL
Cutinase activity assay
PaperBrockmeier U, Caspers M, Freudl R, et al. Systematic screening of all signal peptides from Bacillus subtilis: A powerful strategy in optimizing heterologous protein secretion in gram-positive bacteria[J]. Journal of Molecular Biology, 2006, 362(3): 393-402. PMID16930615 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/16930615/
RECORD: Rec_0112991 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
152.0 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_0184760 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 Cutinase secretion
Corynebacterium glutamicum
9.2 U/mL
Cutinase activity assay
PaperHemmerich J, Rohe P, Kleine B, et al. Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum[J]. Microbial Cell Factories, 2016, 15(1): 208. PMID27927208 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27927208/
RECORD: Rec_0189515 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
211.7 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_0269156 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 Lipase A secretion
Bacillus subtilis WB600
1.38 U/mL
Lipase activity assay
PaperLingLi Zeng.Effects of different signal peptides on the secretion of lipase A in Bacillus subtilis[D]. Jiangnan University, 2009. (in Chinese)
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