View bacteriocin : Carnobacteriocin B2 (Carnocin CP52)

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[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 19-56, STRAIN=LV17B
MEDLINE=94216339;PubMed=8163526;
Quadri L.E.N., Sailer M., Roy K.L., Vederas J.C., Stiles M.E.
"Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B.", J. Biol. Chem. 269:12204-12211(1994).

[Ref. 2] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=CP5
MEDLINE=98063519;PubMed=9353214;DOI=10.1007/s002849900262
Herbin S., Mathieu F., Brule F., Branlant C., Lefebvre G., Lebrihi A.
"Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese.", Curr. Microbiol. 35:319-326(1997).

[Ref. 3] | View abstract | Export citation
STRUCTURE BY NMR OF 19-66.
MEDLINE=20039867;PubMed=10569926;DOI=10.1021/bi991351x
Wang Y., Henz M.E., Gallagher N.L.F., Chai S., Gibbs A.C., Yan L.Z., Stiles M.E., Wishart D.S., Vederas J.C.
"Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria.", Biochemistry 38:15438-15447(1999).

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End Note
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BibTeX
Sequence
 ........10 ........20 ........30 ........40 ........50 
          |          |          |          |          | 
 VNYGNGVSCS KTKCSVNWGQ AFQERYTAGI NSFVSGVASG AGSIGRRP
Wheel representation
Structure
Composition
Formula C213 H332 N66 O68 S2
Absent amino acids DHLM
Common amino acids G
Mass (Da) 4988.27
Net charge +4
Isoelectric point 9.96
Basic residues 5
Acidic residues 1
Hydrophobic residues 14
Polar residues 25
Aliphatic residues 7
Tiny residues 19
Boman Index -73.88
Hydropathy Index -0.28
Aliphatic Index 54.79
Instability Index 18.67 (stable)
Half Life Mammalian : 100 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 8605 M-1 cm-1
Absorbance 280nm 183.09
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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