Bacteriocin: cinnamycin (Lanthiopeptin)

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Bacteriocin: cinnamycin (Lanthiopeptin)

Accession: BAC010

Classification
Class: Lantibiotic
Genetics
Gene: cinA; Synonyms=rocA
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.
Uniprot and PDB links

UniProt Entry: P29827

PDB Entry2DDE resolved by NMR

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).
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).
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).
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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Gene structure
genome of cinnamycin (Lanthiopeptin)

Gene idNameDescriptionLocation
BACGene7rocAlantibiotic Ro 09-19822..258
rocA
Protein sequence
 ........10 ........20 
          |          | 
 CRQSCSFGPF TFVCDGNTK

Wheel representation
wheel representation of cinnamycin (Lanthiopeptin)
3D Structure
Protein sequence annotations
Features of cinnamycin (Lanthiopeptin)

D
FeaturePosition(s)LengthDescription
PEPTIDE1↔1919
Lantibiotic cinnamycin.
Feature identifier = PRO_0000017149.
Modified residue15(3R)-3-hydroxyaspartate.
Cross-link1↔1818Beta-methyllanthionine (Cys-Thr).
Cross-link4↔1411Lanthionine (Ser-Cys).
Cross-link5↔117Beta-methyllanthionine (Cys-Thr).
Cross-link6↔1914Lysinoalanine (Ser-Lys).
STRAND6↔138
Composition
Hydrophobicity

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

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