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MYP_122298
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Basic Information
YxiT 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
Standard
32 amino acids
C161H255N39O39S2
Standard
Sequence
MKWNNMLKAAGIAVLLFSVFAYAAPSLKAVQA
Physicochemical Analysis
3425.11 Da
10.00
2.50
2.27
0.0780
0.88
0.36
0.37
25.02
113.12
0.1250
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
1240.44
-7.03
42.0
44.0
110.0
241.0
6.0
34.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0078753 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
114.2 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_0173574 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
9.4 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_0311714 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
0.9 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_0411910 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
62.9 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/