Antimicrobial Peptide AP02433

     
 

APD ID:

AP02433

 
 

Name/Class:

Carnolysin (two-component lantibiotic, bacteriocin, UCSS2b; Lactic acid; Gram-positive bacteria, prokaryotes; XTT6; XXW5; XXD6)

 
 

Source:

Carnobacterium maltaromaticum C2

 
 

Sequence:

GDINGEFTTSPACVYSVMVVSKASSAKCAAGASAVSGAILSAIRC

 
 

Length:

45

 
 

Net charge:

1

 
 

Hydrophobic residue%:

51%

 
 

Boman Index:

0.25 kcal/mol

 
 

3D Structure:

Unknown

 
 

SwissProt ID:

Reference ID: Ref  

 
 

Activity:

Anti-Gram+,

 
 

Crucial residues:

 
 

Additional info:

This is a two-component lantibiotic. The sequence of Carnolysin A1 is provided in the sequence field. The sequence of Carnolysin A2 is GDVMPESTPICAGFATLMSSIGLVKTIKGKC. Both sequences are processed after post-translation. Altogether, there are six dehydrated ser or thr, and five thioether bonds in the two chains. For Carnolysin A1, residues 8, 10, and 25 are dehydrated; thioether bonds exist between residues 9, 13; 24,28; 41,45; residues 16, 21, 33, 36, are D-amino acids. For Carnolysin A2, residues 8, 16, and 20 are dehydrated; thioether bonds exist between 7, 11; 26, 31; residues 16 and 19 are D-amino acids, which is the first D-Abu in ribosomally synthesized peptide (Lohans CT et al. 2014). However, further processing appeared to be required to generate active peptides, for example, digestion with endoproteinase GluC. The digested peptides were active against L. lactis, E. faecium, and C. maltaromaticum. Reg. 9/18/2014.

 
       
 

Title:

Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2.

 
 

Author:

Tulini FL, Lohans CT, Bordon KC, Zheng J, Arantes EC, Vederas JC, De Martinis EC.2014

 
 

Reference:

Int J Food Microbiol. 2014 Mar 3;173:81-8. doi: 10.1016/j.ijfoodmicro.2013.12.019. PubMed

 
       

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