View bacteriocin : Cinnamycin (Lanthiopeptin)

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Accession BAC010
Name Cinnamycin (Lanthiopeptin)
Gene cinA; Synonyms=rocA
Class Lantibiotic
Producer Organism Streptoverticillium griseoverticillatum [Gram-positive]
Taxonomy BacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
Target organisms Bacillus
Swiss-Prot Entry P29827
PDB Entry 2DDE resolved by NMR
Other databases EMBL X58545PIR A45767PIR S17181
Description Mode of action:
Can act as inhibitor of the enzyme phospholipase A2, and of the angiotensin-converting enzyme. Shows inhibitory activities against herpes simplex virus and immunopotentiating activities. Its antimicrobial activities are not very pronounced.

Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor.
[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=MAR 164C-MY6
MEDLINE=91301152;PubMed=2070795;
Kaletta C., Entian K.-D., Jung G.
"Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene of a duramycin-type lantibiotic.", Eur. J. Biochem. 199:411-415(1991).

[Ref. 2] | View abstract | Export citation
PROTEIN SEQUENCE OF 60-78.
MEDLINE=91107436;PubMed=2125590;
Fredenhagen A., Fendrich G., Marki F., Marki W., Gruner J., Raschdorf F., Peter H.H.
"Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin.", J. Antibiot. 43:1403-1412(1990).

[Ref. 3] | View abstract | Export citation
PROTEIN SEQUENCE OF 60-78.
MEDLINE=89291558;PubMed=2544544;
Naruse N., Tenmyo O., Tomita K., Konishi M., Miyaki T., Kawaguchi H., Fukase K., Wakamiya T., Shiba T.
"Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin.", J. Antibiot. 42:837-845(1989).

[Ref. 4] | View abstract | Export citation
PROTEIN STRUCTURE.
PubMed=8882709;
Hosoda, K., Ohya, M., Kohno, T., Maeda, T., Endo, S., Wakamatsu, K.
"Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1", J.Biochem.(Tokyo) (1996) 119: 226-230.

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Sequence
 ........10 ........20 
          |          | 
 CRQSCSFGPF TFVCDGNTK
Wheel representation
Structure
Composition
Formula C89 H133 N25 O28 S3
Absent amino acids AEHILMWY
Common amino acids CF
Mass (Da) 2115.66
Net charge +1
Isoelectric point 8.05
Basic residues 2
Acidic residues 1
Hydrophobic residues 4
Polar residues 10
Aliphatic residues 1
Tiny residues 4
Boman Index -34.61
Hydropathy Index -0.22
Aliphatic Index 15.26
Instability Index 77.73 (unstable)
Half Life Mammalian : 1.2 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 125 M-1 cm-1
Absorbance 280nm 6.94
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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