General Information
-
DRAMP ID
- DRAMP00348
-
Peptide Name
- Non-specific lipid-transfer protein 4.1 (LTP 4.1; CW-21; Plants)
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Source
- Hordeum vulgare (Barley)
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Family
- Belongs to the plant LTP family
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Gene
- LTP4.1
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Sequence
- AISCGQVSSALSPCISYARGNGAKPPAACCSGVKRLAGAAQSTADKQAACKCIKSAAGGLNAGKAAGIPSMCGVSVPYAISASVDCSKIR
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Sequence Length
- 90
-
UniProt Entry
- Q43767
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Antifungal
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Target Organism
-
- Fungi: Fusarim solani (EC50=3-20×10-6 M), Pseudomonas solanacearum (EC50=3-6×10-7 M), Pythium aphanidermatum, Clavibacter michiganensis subsp. Sepedonicus (EC50=l-3×10-7 M).
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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
- Lipid-binding
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
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Nonterminal Modifications and Unusual Amino Acids
- Not included yet
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Stereochemistry
- Not included yet
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP00348.
Physicochemical Information
-
Formula
- C362H611N111O116S9
Absent Amino Acids
- EFHW
Common Amino Acids
- A
Mass
- 8663.05
PI
- 9.33
Basic Residues
- 10
Acidic Residues
- 2
Hydrophobic Residues
- 33
Net Charge
- +8
-
Boman Index
- -57.14
Hydrophobicity
- 0.272
Aliphatic Index
- 76.22
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 3480
Absorbance 280nm
- 39.1
Polar Residues
- 36
DRAMP00348
Comments Information
Function
- Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
PTM
- Contains four disulfide bonds 4-52; 14-29; 30-72; 50-86.
Literature Information
- ·Literature 1
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Title
- Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens.
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Pubmed ID
- 8420795
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Reference
- FEBS Lett. 1993 Jan 25;316(2):119-122.
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Author
- Molina A, Segura A, García-Olmedo F.
- ·Literature 2
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Title
- Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins.
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Pubmed ID
- 8281190
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Reference
- Plant J. 1993 Dec;4(6):983-991.
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Author
- Molina A, Garca-Olmedo F.