Peptide Database

Peptide NamewapA signal peptide

Function Ontology

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 ▸ Lipase

Standard StatusStandard

Sequence Length32 amino acids

Chemical FormulaC173H295N49O37S2

DescriptionStandard

        MKKRKRRNFKRFIAAFLVLALMISLVPADVLA
    

Molecular Weight3717.63 Da

Isoelectric Point (pI)12.00

Net Charge (pH 7.0)6.50

Net Charge (pH 7.4) 6.28

Charge Density (pH 7.0) 0.2030

GRAVY Index0.59

Hydrophobic Moment 0.77

Boman Index0.04

Instability Index62.00

Aliphatic Index 128.12

Aromaticity 0.0938

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 1408.93

LogP -6.53

H-bond Donors 51.0

H-bond Acceptors 46.0

Rotatable Bonds 128.0

Heavy Atoms 261.0

Ring Count 4.0

Amide Bonds 32.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0086590 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

Activity14331.45 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_0132894 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus subtilis [Bacterium]

FamilySignal 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 Lipase A secretion

TargetBacillus subtilis WB600

Activity0.18 U/mL

MethodLipase activity assay

RECORD: Rec_0222927 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus subtilis [Bacterium]

FamilyTat 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 Cutinase secretion

TargetBacillus subtilis TEB1030

Activity2.88 U/mL

MethodCutinase 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_0342827 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

Activity95.56 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_0366259 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus subtilis [Bacterium]

FamilyTat 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 L-Asparaginase secretion

TargetBacillus subtilis WB600

Activity28.9 U/mL

MethodAsparaginase activity assay

PaperFeng Y, Liu S, Jiao Y, et al. Enhanced extracellular production of L-asparaginase from Bacillus subtilis 168 by B-subtilis WB600 through a combined strategy[J]. Applied Microbiology and Biotechnology, 2017, 101(4): 1509-1520 PMID27796436 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/27796436/