View bacteriocin : subtilosin Bookmark and Share

[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], STRAIN=168
MEDLINE=98044033;PubMed=9384377;DOI=10.1038/36786
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter
"?",

[Ref. 2] | View abstract | Export citation
IDENTIFICATION, AND INDUCTION, STRAIN=168 / JH642
MEDLINE=20270159;PubMed=10809709;DOI=10.1128/JB.182.11.3266-3273.2000
Zheng G., Hehn R., Zuber P.
"Mutational analysis of the sbo-alb locus of Bacillus subtilis: identification of genes required for subtilosin production and immunity.", J. Bacteriol. 182:3266-3273(2000).

[Ref. 3] | View abstract | Export citation
FUNCTION
PubMed=17213266;
Shelburne CE, An FY, Dholpe V, Ramamoorthy A, Lopatin DE, Lantz MS.
"The spectrum of antimicrobial activity of the bacteriocin subtilosin A.", J Antimicrob Chemother. 2007 Feb;59(2):297-300.

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Sequence
........10........20........30........40........50........60
| | | | | |
MKLPVQQVYSVYGGKDLPKGHSHSTMPFLSKLQFLTKIYLLDIHTQPFFI

Wheel representation
Composition
AA %

AA %

AA %
Ala 0 .00%

Ile 3 6.00%

Arg 0 .00%
Cys 0 .00%

Lys 5 10.00%

Ser 4 8.00%
Asp 2 4.00%

Leu 7 14.00%

Thr 3 6.00%
Glu 0 .00%

Met 2 4.00%

Val 3 6.00%
Phe 4 8.00%

Asn 0 .00%

Trp 0 .00%
Gly 3 6.00%

Pro 4 8.00%

Tyr 3 6.00%
His 3 6.00%

Gln 4 8.00%
Total 50
Formula C274 H421 N65 O69 S2
Absent amino acids ACENRW
Common amino acids L
Mass (Da) 5812.7
Net charge +6
Isoelectric point 10.01
Basic residues 8
Acidic residues 2
Hydrophobic residues 17
Polar residues 13
Aliphatic residues 13
Tiny residues 7
Boman Index -22.3
Hydropathy Index 0.02
Aliphatic Index 95.4
Instability Index 37.77 (stable)
Half Life Mammalian : 30 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 4470 M-1 cm-1
Absorbance 280nm 91.22
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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