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MYP_097199
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Basic Information
yvpB signal peptide
Annotation / Sequence feature ▸ Signal peptide
Biotechnology / Production and expression ▸ Secretory enzyme production ▸ Cutinase secretion
Biotechnology / Production and expression ▸ Secretory expression optimization
Enzyme modulation ▸ Enzyme inhibition ▸ Amylase inhibition ▸ Alpha-amylase inhibitory
Standard
25 amino acids
C129H220N30O31S3
Standard
Sequence
MKTLRTLCVLMILSGVIFFGLKIDA
Physicochemical Analysis
2783.50 Da
9.30
1.49
1.26
0.0596
1.43
0.44
0.42
15.20
152.00
0.0800
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
973.65
-3.33
36.0
36.0
95.0
193.0
2.0
24.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0024162 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
0.0 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_0088253 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
29.7 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_0254227 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_0255116 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
1.6 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/