Peptide Database

Peptide NamematE 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

Enzyme / Catalytic activity ▸ Protease ▸ Bacillus protease novo type (BPN') secretion

Standard StatusStandard

Sequence Length31 amino acids

Chemical FormulaC155H279N47O38S4

DescriptionStandard

        MRMKRLRMRKHLLIAVCTLALLLSSPIVSDA
    

Molecular Weight3537.43 Da

Isoelectric Point (pI)11.56

Net Charge (pH 7.0)4.58

Net Charge (pH 7.4) 4.29

Charge Density (pH 7.0) 0.1476

GRAVY Index0.66

Hydrophobic Moment 0.30

Boman Index0.05

Instability Index49.71

Aliphatic Index 141.61

Aromaticity 0.0000

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 1374.07

LogP -9.47

H-bond Donors 52.0

H-bond Acceptors 48.0

Rotatable Bonds 122.0

Heavy Atoms 244.0

Ring Count 2.0

Amide Bonds 30.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0266174 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus licheniformis [Bacterium]

FamilyTat signal peptide

Tax ID1402

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

Activity14158.17 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_0363533 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus licheniformis DSM 13 = ATCC 14580 [Bacterium]

FamilySec signal peptide

Tax ID279010

Structure & Mods

Configlinear signal peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Protein secretion signal peptide Secretory expression optimization Bacillus protease novo type (BPN') secretion

TargetBacillus subtilis TEB1030

Activity3.58 U/mL

MethodProtease activity assay

PaperDegering C, Eggert T, Puls M, et al. Optimization of Protease Secretion in Bacillus subtilis and Bacillus licheniformis by Screening of Homologous and Heterologous Signal Peptides[J]. Applied and Environmental Microbiology, 2010, 76(19): 6370-6376. PMID20709850 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20709850/

RECORD: Rec_0404449 VERIFIED: YES

Provenance & Taxonomy

OrganismBacillus licheniformis [Bacterium]

FamilyTat signal peptide

Tax ID1402

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

Activity5160.24 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/