View bacteriocin : thuricin-S Bookmark and Share

Accession BAC009
Name thuricin-S
Related Entries thuricin-17
Gene Unidentified
Class Unclassified
Producer Organism Bacillus thuringiensis subsp, entomocidus [Gram-positive]
Taxonomy BacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group
Target organisms Gram-positive bacteria : Listeria monocytogenes - Bacillus subtilis -

other Bacillus - Enterobacter cloacae - Lactobacillus acidophilus - Lactobacillus lactis - Pediococcus acidolactici - Streptococcus thermophilus -

Gram-negative bacteria : Spirillum cholerae - Shigella flexneri - Pseudomonas aeruginosa
Swiss-Prot Entry P84763
PDB Entry Unknown
[Ref. 1]
PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY, STRAIN=HD198

Chehimi S., Delalande F., Sable S., Hajlaoui M.R., Van Dorsselaer A., Limam F., Pons A.M.
"Purification and partial amino acid sequence of thuricin S, a new anti-Listeria bacteriocin from Bacillus thuringiensis.", Submitted (JAN-2006) to Swiss-Prot.

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Sequence
........10........20
| |
DWTXWSXLVXAACSVELL

Warning: Partial sequence.
Wheel representation
Composition
AA N° %

AA N° %

AA N° %
Ala 2 11.11%

Ile 0 .00%

Arg 0 .00%
Cys 1 5.56%

Lys 0 .00%

Ser 2 11.11%
Asp 1 5.56%

Leu 3 16.67%

Thr 1 5.56%
Glu 1 5.56%

Met 0 .00%

Val 2 11.11%
Phe 0 .00%

Asn 0 .00%

Trp 2 11.11%
Gly 0 .00%

Pro 0 .00%

Tyr 0 .00%
His 0 .00%

Gln 0 .00%

Xaa 3 16.67%
Total 18
Formula C78 H111 N17 O20 S1
Absent amino acids FGHIKMNPQRY
Common amino acids LX
Mass (Da) 1987.2
Net charge -2
Isoelectric point 3.55
Basic residues 0
Acidic residues 2
Hydrophobic residues 9
Polar residues 4
Aliphatic residues 5
Tiny residues 4
Boman Index 7.5
Hydropathy Index 0.82
Aliphatic Index 108.33
Instability Index 22.17 (stable)
Half Life Mammalian : 1.1 hour
Yeast : 3 min
E. coli : >10 hour
Extinction Coefficient 11000 M-1 cm-1
Absorbance 280nm 647.06
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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