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MYP_122438
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Basic Information
ywmC 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
23 amino acids
C119H194N28O28S3
Standard
Sequence
MKKRFSLIMMTGLLFGLTSPAFA
Physicochemical Analysis
2561.18 Da
11.17
2.50
2.28
0.1086
0.86
0.36
0.32
45.02
93.48
0.1304
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
889.59
-4.64
32.0
34.0
85.0
178.0
4.0
22.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0034204 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
25.5 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_0081625 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
4.6 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_0133636 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
1.17 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_0323125 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
56.9 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_0338725 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 subtilis WB600
1050.36 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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