View bacteriocin : Enterocin A Bookmark and Share

[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE, STRAIN=CTC492
MEDLINE=96209231;PubMed=8633865;
Aymerich T., Holo H., Havarstein L.S., Hugas M., Garriga M., Nes I.F.
"Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins.", Appl. Environ. Microbiol. 62:1676-1682(1996).

[Ref. 2]
NUCLEOTIDE SEQUENCE, STRAIN=CTC492

Harvarstein L.
"", Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.

[Ref. 3]
NUCLEOTIDE SEQUENCE, STRAIN=N15

Uchiyama K., Losteinkit C., Shioya S.
"Characterization of bacteriocin produced by Enterococcus faecium N15 and cloning of the related genes.", Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.

[Ref. 4] | View abstract | Export citation
NUCLEOTIDE SEQUENCE, STRAIN=DPC1146
MEDLINE=99203104;PubMed=10103244;
O'Keeffe T., Hill C., Ross R.P.
"Characterization and heterologous expression of the genes encoding enterocin A production, immunity, and regulation in Enterococcus faecium DPC1146.", Appl. Environ. Microbiol. 65:1506-1515(1999).

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Sequence
........10........20........30........40........50
| | | | |
TTHSGKYYGNGVYCTKNKCTVDWAKATTCIAGMSIGGFLGGAIPGKC

Wheel representation
Composition
AA %

AA %

AA %
Ala 4 8.51%

Ile 3 6.38%

Arg 0 .00%
Cys 4 8.51%

Lys 5 10.64%

Ser 2 4.26%
Asp 1 2.13%

Leu 1 2.13%

Thr 6 12.77%
Glu 0 .00%

Met 1 2.13%

Val 2 4.26%
Phe 1 2.13%

Asn 2 4.26%

Trp 1 2.13%
Gly 9 19.15%

Pro 1 2.13%

Tyr 3 6.38%
His 1 2.13%

Gln 0 .00%
Total 47
Formula C211 H329 N57 O63 S5
Absent amino acids EQR
Common amino acids G
Mass (Da) 4851.38
Net charge +5
Isoelectric point 8.98
Basic residues 6
Acidic residues 1
Hydrophobic residues 12
Polar residues 26
Aliphatic residues 6
Tiny residues 15
Boman Index -20.81
Hydropathy Index -0.03
Aliphatic Index 54.04
Instability Index 25.08 (stable)
Half Life Mammalian : 7.2 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 10220 M-1 cm-1
Absorbance 280nm 222.17
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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