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MYP_086796
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Basic Information
yhdC 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
Standard
21 amino acids
C107H178N22O26S3
Standard
Sequence
MKSLPYTIALLFCGLIIVSMA
Physicochemical Analysis
2284.88 Da
7.95
0.49
0.26
0.0233
1.72
0.33
0.59
16.49
153.33
0.0952
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
743.47
-1.63
27.0
30.0
73.0
158.0
3.0
20.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0098506 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
49.1 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_0315517 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
65.5 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_0319587 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
8609.0 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_0345117 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
0.0 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_0368555 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
5167.88 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/