Peptide Database

Peptide NameyjdB signal peptide

Function Ontology

Annotation / Sequence feature ▸ Signal peptide

Biotechnology / Production and expression ▸ Secretory enzyme production ▸ Alkaline protease secretion

Biotechnology / Production and expression ▸ Secretory expression optimization

Standard StatusStandard

Sequence Length27 amino acids

Chemical FormulaC119H202N32O36S

DescriptionStandard

        MNFKKTVVSALSISALALSVSGVASAH
    

Molecular Weight2689.13 Da

Isoelectric Point (pI)10.00

Net Charge (pH 7.0)1.59

Net Charge (pH 7.4) 1.32

Charge Density (pH 7.0) 0.0587

GRAVY Index0.96

Hydrophobic Moment 0.42

Boman Index0.33

Instability Index-4.65

Aliphatic Index 119.26

Aromaticity 0.0370

Extinction Coeff. Reduced 0.00

Extinction Coeff. Oxidized 0.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 1085.34

LogP -13.03

H-bond Donors 39.0

H-bond Acceptors 40.0

Rotatable Bonds 89.0

Heavy Atoms 188.0

Ring Count 2.0

Amide Bonds 27.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0017844 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus subtilis [Bacterium]

FamilySec signal peptide

Tax ID1423

Structure & Mods

Configlinear signal peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Protein secretion signal peptide Secretory expression optimization Alkalineprotease (alk) secretion

TargetBacillus amyloliquefaciens 111018

Activity9778.97 U/mL

MethodProtease 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_0235405 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus subtilis subsp. subtilis str. 168 [Bacterium]

FamilySec signal peptide

Tax ID224308

Structure & Mods

Configlinear signal peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Protein secretion signal peptide Secretory expression optimization Alkalineprotease (alk) secretion

TargetBacillus subtilis WB600

Activity959.0 U/mL

MethodProtease 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_0296139 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus subtilis subsp. subtilis str. 168 [Bacterium]

FamilySec signal peptide

Tax ID224308

Structure & Mods

Configlinear signal peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Protein secretion signal peptide Secretory expression optimization Alkalineprotease (alk) secretion

TargetBacillus amyloliquefaciens 111018

Activity5952.75 U/mL

MethodProtease 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/