General Information
-
DRAMP ID
- DRAMP03532
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Peptide Name
- Moricin-1 (Insects, animals)
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Source
- Bombyx mori (Silk moth)
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Family
- Belongs to the moricin family
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Gene
- MOR1
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Sequence
- AKIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLKPKKRKH
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Sequence Length
- 42
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UniProt Entry
- P82818
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Protein Existence
- Protein level
Activity Information
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Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
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Target Organism
-
- Gram-negative bacteria: Escherichia coli JM109 (MIC=0.31 µM), Acinetobacter sp. NISL B-4653 (MIC=0.27 µM), Pseudomonas fluorescens IAM1179 (MIC=0.53 µM), Pseudomonas aeruginosa IAM15140 (MIC=0.81 µM);
- Gram-positive bacteria: Bacillus subtilis IAM1107 (MIC=0.19 µM), Bacillus megaterium IAM1030 (MI=0.09 µM), Bacillus cereus IFO3457 (MIC=0.38 µM), Staphylococcus aureus ATCC6538P (MIC=0.21 µM), Staphylococcus aureus ATCC6538P (MIC=0.22 µM), Staphylococcus aureus IFO3083 (MIC=0.46 µM), Staphylococcus xylosus IAM1312 (MIC=0.27 µM), Staphylococcus epidermidis IFO12993 (MIC=0.18 µM), Streptococcus pyogenes ATCC21547 (MIC=0.25 µM).
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Linear
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N-terminal Modification
- Free
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C-terminal Modification
- Free
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Nonterminal Modifications and Unusual Amino Acids
- Free
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Stereochemistry
- L
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Structure
- Alpha helix (1 helices; 30 residues)
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Structure Description
- The solution structure reveals an unique structure comprising of a long alpha-helix containing eight turns along nearly the full length of the peptide except for four N-terminal residues and six C-terminal residues. The electrostatic surface map shows that the N-terminal segment of the alpha-helix, residues 5-22, is an amphipathic alpha-helix with a clear separation of hydrophobic and hydrophilic faces, and that the C-terminal segment o
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Helical Wheel Diagram
-
PDB ID
- 1KV4 resolved by NMR.
- 1KV4-> 
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Predicted Structure
- Please click DRAMP03532_predicted_structure.pdb to download.
Physicochemical Information
-
Formula
- C208H358N62O51
Absent Amino Acids
- CEMQWY
Common Amino Acids
- K
Mass
- 4543.52
PI
- 11.36
Basic Residues
- 12
Acidic Residues
- 1
Hydrophobic Residues
- 18
Net Charge
- +11
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Boman Index
- -55.43
Hydrophobicity
- -0.21
Aliphatic Index
- 100
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 0
Absorbance 280nm
- 0
Polar Residues
- 9
DRAMP03532
Comments Information
Function
- Has antibacterial activity against Gram-positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure.
Literature Information
- ·Literature 1
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Title
- Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori.
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Pubmed ID
- 8530391
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Reference
- J Biol Chem. 1995 Dec 15;270(50):29923-29927.
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Author
- Hara S, Yamakawa M.
- ·Literature 2
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Title
- Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori.
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Pubmed ID
- 11997013
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Reference
- FEBS Lett. 2002 May 8;518(1-3):33-38.
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Author
- Hemmi H, Ishibashi J, Hara S, Yamakawa M.