• • DRAMP ID

  • DRAMP00170

• • Peptide Name

  • Carnocyclin A (CclA; Bacteriocin)

• • Source

  • Carnobacterium maltaromaticum UAL307 (Gram-positive bacteria)

• • Family

  • Belongs to the class IIc bacteriocin

• • Gene

  • cclA

• • Sequence

  • LVAYGIAQGTAEKVVSLINAGLTVGSIISILGGVTVGLSGVFTAVKAAIAKQGIKKAIQL

• • Sequence Length

  • 60

• • UniProt Entry

  • B2MVM5

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+

• • Target Organism

  • • Gram-positive bacteria:

      Target Organism	Activity
      Carnobacterium maltaromaticum UAL26	-
      C. maltaromaticum LV17A	-
      C. divergens LV13	-
      Brochothrix campestris ATCC 43754	-
      B. thermosphacta ATCC 11509	-
      Enterococcus faecalis ATCC 7080	-
      E. faecium ATCC 19434	-
      E. faecium BFE900	-
      Lactococcus lactis subsp. lactis ATCC 11454	-
      Lactococcus lactis subsp. cremoris ATCC 11602	-
      Lactococcus lactis subsp. lactis DPC3147	-
      Lactobacillus sakeii 706	-
      L. sakei UAL1218	-
      Leuconostoc mesenteroides Y105	-
      Pediococcus acidilactici PAC1.0	-
      Listeria monocytogenes ATCC 15313	-
      Listeria monocytogenes H7762	-
      Listeria monocytogenes ATCC 43256	-
      Listeria monocytogenes HPB 642	-
      Listeria monocytogenes UAFM 1	-
      Listeria monocytogenes UAFM 15	-
      Staphylococcus aureus ATCC 25923	-
      Staphylococcus aureus ATCC 6538	-
      Staphylococcus aureus ATCC 29213	-

• • Hemolytic Activity

  • • No hemolysis information or data found in the reference(s) presented in this entry

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • Lipid II

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • No specific N-terminal

• • C-terminal Modification

  • No specific C-terminal

• • Nonterminal Modifications and Unusual Amino Acids

  • None

• • Stereochemistry

  • L

• • Structure

  • Alpha helix (4 helices; 38 residues)

• • Structure Description

  • The NMR study results reveal that CclA preferentially binds halide anions and has a structure that is surprisingly similar to that of AS-48 despite low sequence identity, different oligomeric state, and disparate function. CclA folds into a compact globular bundle, comprised of four helices surrounding a hydrophobic core.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2KJF resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP00170.

DRAMP00170

• • Function

  • Carnocyclin A (CclA) is a potent antimicrobial peptide from Carnobacterium maltaromaticum UAL307 that displays a broad spectrum of activity against numerous Gram-positive organisms.

• • Biophysicochemical properties

  • pH dependence (Stable from pH 2 to 12); Temperature dependence (Displays a high degree of stability when incubated at temperatures between -80 and 75 degrees Celsius for 60 minutes. Autoclaving the peptide at 121 degrees Celsius for 15 minutes had no effect but incubation at 100 degrees Celsius for 60 minutes caused a 32-fold reduction in activity).

• ·Literature 1

• • Title

  • Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307.

• • Pubmed ID

  • 18552180

• • Reference

  • Appl Environ Microbiol. 2008 Aug;74(15):4756-4763.

• • Author

  • Martin-Visscher LA, van Belkum MJ, Garneau-Tsodikova S, Whittal RM, Zheng J, McMullen LM, Vederas JC.

• ·Literature 2

• • Title

  • The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif.

• • Pubmed ID

  • 19692336

• • Reference

  • J Biol Chem. 2009 Oct 16;284(42):28674-81.

• • Author

  • Martin-Visscher LA, Gong X, Duszyk M, Vederas JC.