View bacteriocin : curvacin-A Bookmark and Share

[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=LTH1174
MEDLINE=94058500;PubMed=7694558;DOI=10.1007/BF00292077
Tichaczek P.S., Vogel R.F., Hammes W.P.
"Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174.", Arch. Microbiol. 160:279-283(1993).

[Ref. 2]
PRELIMINARY PARTIAL PROTEIN SEQUENCE OF 19-59, STRAIN=LTH1174

Tichaczek P.S., Nissen-Meyer J., Nes I.F., Vogel R.F., Hammes W.P.
"Characterization of the bacteriocins curvacin A from Lactobacillus curvatus LTH1174 and sakacin P from L. sake LTH673.", Syst. Appl. Microbiol. 15:460-465(1992).

[Ref. 3] | View abstract | Export citation
Mutational Analysis / Structure-function relationships
PubMed=18791005;DOI=10.1128/AEM.01068-08
Haugen HS, Kristiansen PE, Fimland G, Nissen-Meyer J
"Mutational Analysis of the Class IIa Bacteriocin Curvacin A and Its Orientation in Target Cell Membranes.", Appl. Environ. Microbiol. 74(21):6766-73 (2008).

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

Wheel representation
Structure
Composition
AA %

AA %

AA %
Ala 4 9.76%

Ile 3 7.32%

Arg 2 4.88%
Cys 2 4.88%

Lys 2 4.88%

Ser 4 9.76%
Asp 0 .00%

Leu 1 2.44%

Thr 1 2.44%
Glu 1 2.44%

Met 2 4.88%

Val 2 4.88%
Phe 0 .00%

Asn 4 9.76%

Trp 2 4.88%
Gly 8 19.51%

Pro 0 .00%

Tyr 2 4.88%
His 0 .00%

Gln 1 2.44%
Total 41
Formula C184 H288 N56 O56 S4
Absent amino acids DFHP
Common amino acids G
Mass (Da) 4327.58
Net charge +3
Isoelectric point 9.37
Basic residues 4
Acidic residues 1
Hydrophobic residues 12
Polar residues 21
Aliphatic residues 6
Tiny residues 16
Boman Index -41.86
Hydropathy Index -0.19
Aliphatic Index 61.95
Instability Index 27.63 (stable)
Half Life Mammalian : 4.4 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 14105 M-1 cm-1
Absorbance 280nm 352.63
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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