Peptide Database

Peptide NameyvbX 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

Standard StatusStandard

Sequence Length27 amino acids

Chemical FormulaC144H238N32O33S2

DescriptionStandard

        MKKWLIIAVSLAIAIVLFMYTKGEAKA
    

Molecular Weight3009.75 Da

Isoelectric Point (pI)9.82

Net Charge (pH 7.0)2.50

Net Charge (pH 7.4) 2.27

Charge Density (pH 7.0) 0.0925

GRAVY Index1.12

Hydrophobic Moment 0.30

Boman Index0.41

Instability Index10.74

Aliphatic Index 141.11

Aromaticity 0.1111

Extinction Coeff. Reduced 6990.00

Extinction Coeff. Oxidized 6990.00

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

Amino Acid Composition

TPSA 1037.78

LogP -1.46

H-bond Donors 37.0

H-bond Acceptors 38.0

Rotatable Bonds 102.0

Heavy Atoms 211.0

Ring Count 4.0

Amide Bonds 26.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0147274 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 Cutinase secretion

TargetBacillus subtilis TEB1030

Activity1.09 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_0332057 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

Activity146.53 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_0381178 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

Activity7154.3 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_0413051 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

Activity1039.69 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/