Peptide Database

Peptide Nameendo-1,4-beta-xylanase 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 Length29 amino acids

Chemical FormulaC141H230N32O37S2

DescriptionStandard

        MFKFVTKVLTVVIAATISFCLSAVPASAN
    

Molecular Weight3029.66 Da

Isoelectric Point (pI)9.31

Net Charge (pH 7.0)1.49

Net Charge (pH 7.4) 1.26

Charge Density (pH 7.0) 0.0513

GRAVY Index1.45

Hydrophobic Moment 0.58

Boman Index0.47

Instability Index18.54

Aliphatic Index 121.03

Aromaticity 0.1034

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 1085.84

LogP -8.29

H-bond Donors 39.0

H-bond Acceptors 41.0

Rotatable Bonds 95.0

Heavy Atoms 212.0

Ring Count 4.0

Amide Bonds 29.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0051038 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

Activity6115.84 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_0161815 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

Activity6238.16 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_0195318 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

Activity12951.0 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/