View bacteriocin : Hominicin

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Accession BAC183
Name Hominicin
Gene Unidentified
Class lantibiotic
Producer Organism Staphylococcus hominis MBBL 2–9 [Gram-positive]
Taxonomy BacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Target organisms Staphylococcus aureus ATCC 25923 (MIC=0.06µg/ml) - Staphylococcus aureus (MRSA) ATCC 11435 (MIC=0.96µg/ml) - Staphylococcus aureus (vancomycin-intermediate VISA) CCARM 3501 (MIC=3.82µg/ml)
Swiss-Prot Entry No entry found
PDB Entry Unknown
Description Structure: Hominicin is post-translationally modified at its respective 1st, 2nd, 5th, 8th, 15th, and 21st residues. The structural property of hominicin present that this peptide is a Class I variant without thioether bridge. It contains modified amino acids: 2-amino-2-butenoic acid (dhb), N2, N2-dimethyl-1,2-propanediamine (dmp) and N1, N1-dimethyl-isoleucine (DmIle).

Note: Hominicin exhibited heat stability up to 121 °C for 15 min and activity under both acidic and basic conditions (from pH 2.0 to 10.0). [Ref1]
[Ref. 1] | View abstract | Export citation
PROTEIN SEQUENCE, FUNCTION AND MASS SPECTROMETRY
PubMed=20654578;DOI=10.1016/j.bbrc.2010.07.024
Kim PI, Sohng JK, Sung C, Joo HS, Kim EM, Yamaguchi T, Park D, Kim BG.
"Characterization and structure identification of an antimicrobial peptide, hominicin, produced by Staphylococcus hominis MBBL 2–9", Biochem Biophys Res Commun. 399(2):133-8(2010).

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Sequence
 ........10 ........20 ........30 
          |          |          | 
 XTPATPFTPA ITEITAAVIA X
Wheel representation
Composition
Formula C0 H0 N0 O0 S0
Absent amino acids CDGHKLMNQRSWY
Common amino acids TA
Mass (Da) 1
Net charge -1
Isoelectric point 3.85
Basic residues 0
Acidic residues 1
Hydrophobic residues 10
Polar residues 5
Aliphatic residues 4
Tiny residues 5
Boman Index 11.17
Hydropathy Index 0.843
Aliphatic Index 93.33
Instability Index 54.43 (unstable)
Half Life Mammalian : 0
Yeast : 0
E. coli : 0
Extinction Coefficient 0 M-1 cm-1
Absorbance 280nm 0
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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