• DRAMP ID

    • DRAMP03304
    • Peptide Name

    • Hydramacin-1 (Hm-1; annelida, animals)
    • Source

    • Hydra vulgaris (Hydra) (Hydra attenuata)
    • Family

    • Belongs to the macin family
    • Gene

    • Not found
    • Sequence

    • QIVDCWETWSRCTKWSQGGTGTLWKSCNDRCKELGRKRGQCEEKPSRCPLSKKAWTCICY
    • Sequence Length

    • 60
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
    • Target Organism

      • Gram-negative bacteria: Acinetobacter baumannii ATCC 19606 (MBC=7.1 µM), Burkholderia cepacia ATCC 25416 (MBC>14.3 μM),Burkholderia cepacia ATCC 17759 (MBC>14.3 μM), B. cepacia LMG 16654 (MBC>14.3 μM), Citrobacter freundii NCTC 9750 (MBC=7.1 μM), C. freundii C7 (MBC=0.9 μM), Enterobacter cloacae Va11263/03 (MBC>14.3 μM), E. cloacae Va12270/03 (MBC=0.9 μM), Escherichia coli ATCC 25922 (MBC=0.9 μM), Klebsiella pneumoniae ATCC 13883 (MBC=0.9 μM), Klebsiella oxytoca ATCC 13182 (MBC=0.9 μM), Proteus mirabilis ATCC 21100 (MBC=14.3 μM), P. vulgaris ATCC 13315 (MBC>14.3 μM), Providencia rettgeri NCTC 7475 (MBC>14.3 μM), Pseudomonas aeruginosa NCTC 11446 (MBC>14.3 μM), Salmonella typhimurium 10003442 (MBC=0.9 μM), S. typhimurium 10003630 (MBC=0.9 μM), Serratia marcescens Mero060/148 (MBC>14.3 µM), S. marcescens Mero103/013 (MBC>14.3 μM), S. marcescens NCTC 10211 (MBC>14.3 μM), Yersinia enterocolitica NCTC 11176 (MBC=0.9 µM).
      • Multi-resistant Gram-negative bacteria: Escherichia coli Co 86 ESBL (MBC=3.6 μM), Klebsiella oxytoca ESBL 33 (MBC=7.1 µM), K. oxytoca ESBL 37 (MBC=3.6 μM), Klebsiella pneumoniae ATCC 700603 (MBC=3.6 μM).
      • Gram-positive bacteria: Staphylococcus aureus ATCC 6538 (MBC>14.3 μM), Staphylococcus haemolyticus ATCC 29970 (MBC=1.8 μM), Streptococcus pyogenes ATCC 12344 (MBC>14.3 μM).
      • Multi-resistant Gram-positive bacteria: Staphylococcus aureus ATCC 33593 (MRSA) (MBC>14.3 μM), Enterococcus faecalis ATCC 51299 (MBC>14.3 μM).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • cell membrane
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Combine helix and strand structure
    • Structure Description

    • The molecule possesses two short α-helices (residues 10-14 and 27-33) at the N terminus which are separated by a long flexible loop. The C-terminal region contains two β-strands (residues 38-42 and 56-60) in an antiparallel arrangement separated by a long flexible loop.
    • Helical Wheel Diagram

    • DRAMP03304 helical wheel diagram
    • PDB ID

    • 2K35 resolved by NMR.
  • 2K35-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP03304.
    • Formula

    • C300H471N91O88S8
    • Absent Amino Acids

    • FHM
    • Common Amino Acids

    • CK
    • Mass

    • 7017.08
    • PI

    • 9.05
    • Basic Residues

    • 12
    • Acidic Residues

    • 6
    • Hydrophobic Residues

    • 12
    • Net Charge

    • +6
    • Boman Index

    • -154.34
    • Hydrophobicity

    • -0.948
    • Aliphatic Index

    • 39
    • Half Life

      • Mammalian:0.8 hour
      • Yeast:10 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 29490
    • Absorbance 280nm

    • 499.83
    • Polar Residues

    • 25

DRAMP03304

DRAMP03304 chydropathy plot
    • Function

    • Hydramacin-1 is potently active against Gram-positive and Gram-negative bacteria including multi-resistant human pathogenic strains. Is not active against the Gram-positive Coccus species, Gram-negative non-fermentation species and against the fungus C.albicans. It leads to aggregation of bacteria as an initial step of its bactericidal mechanism. Aggregated cells are connected via electron-dense contacts and adopt a thorn apple-like morphology. Hydramycin contains a belt of positively charged residues that separate two hydrophobic areas. This structure may explain the observed aggregation of bacteria, since each of these areas can immerse into the outer leaflets of the membranes of two individual bacteria. Is able to permeabilize membranes of viable bacteria at low and neutral pH values, but no pore-forming activity is not detected.
    • Tissue specificity

    • Expressed in the endodermal epithelium.
    • Induction

    • By bacterial lipopolysaccharides (LPS).
    • PTM

    • Contains four disulfide bonds.
  • ·Literature 1
    • Title

    • Uncovering the evolutionary history of innate immunity: the simple metazoan Hydra uses epithelial cells for host defence.
    • Reference

    • Dev Comp Immunol. 2009 Apr;33(4):559-569.
    • Author

    • Bosch TC, Augustin R, Anton-Erxleben F, Fraune S, Hemmrich G, Zill H, Rosenstiel P, Jacobs G, Schreiber S, Leippe M, Stanisak M, Grötzinger J, Jung S, Podschun R, Bartels J, Harder J, Schröder JM.
  • ·Literature 2
    • Title

    • Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra.
    • Reference

    • J Biol Chem. 2009 Jan 16;284(3):1896-1905.
    • Author

    • Jung S, Dingley AJ, Augustin R, Anton-Erxleben F, Stanisak M, Gelhaus C, Gutsmann T, Hammer MU, Podschun R, Bonvin AM, Leippe M, Bosch TC, Grötzinger J.