Peptide Database

Peptide NameyjfA 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 Length28 amino acids

Chemical FormulaC147H239N35O30S2

DescriptionStandard

        MKRLFMKASLVLFAVVFVFAVKGAPAKA
    

Molecular Weight3040.82 Da

Isoelectric Point (pI)11.33

Net Charge (pH 7.0)4.50

Net Charge (pH 7.4) 4.27

Charge Density (pH 7.0) 0.1606

GRAVY Index1.26

Hydrophobic Moment 0.46

Boman Index0.37

Instability Index27.95

Aliphatic Index 115.00

Aromaticity 0.1429

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 1026.44

LogP -2.59

H-bond Donors 36.0

H-bond Acceptors 37.0

Rotatable Bonds 100.0

Heavy Atoms 214.0

Ring Count 5.0

Amide Bonds 27.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0035490 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

Activity6790.49 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_0169172 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

Activity3.84 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_0220033 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

Activity159.3 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_0235087 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

Activity11365.27 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/