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MYP_018346
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Basic Information
Divercin V41
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Standard
43 amino acids
C201H300N54O57S4
Standard
Sequence
TKYYGNGVYCNSKKCWVDWGQASGCIGQTVVGGWLGGAIPGKC
Physicochemical Analysis
4513.12 Da
8.82
2.35
2.09
0.0547
-0.12
0.37
0.19
5.95
58.84
0.1395
20970.00
21220.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
1779.45
-18.86
66.0
64.0
142.0
316.0
10.0
46.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0139027 VERIFIED: YES
Provenance & Taxonomy
Carnobacterium divergens [Bacterium]
Bacteriocin
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial
Listeria innocua
PMID15205430 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/15205430/
RECORD: Rec_0192911 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 20.9%, E 0.0%, T 44.2%, C 34.9% [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antibacterial Antimicrobial Anti-Gram-positive
PaperBACTIBASE second release: a database and tool platform for bacteriocin characterization PMID20105292 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20105292/
RECORD: Rec_0215600 VERIFIED: NO
Provenance & Taxonomy
synthetic construct [Synthetic]
32630
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
Evidence URLhttps://camp.bicnirrh.res.in/seqDisp.php?id=CAMPSQ7090
RECORD: Rec_0227212 VERIFIED: YES
Provenance & Taxonomy
Carnobacterium divergens [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
The peptide became inactive after Trp oxidation or disulfide bond reduction. Segment 18-43 is active. The recombinant form contains 4 more residues (AMDP) at the N-terminus. Single-residue mutants of DvnRV41 were found to be less active than DvnRV41 (Rihakova J et al. 2009 ). Chemical modification: the peptide lost activity when S-S bonds were disrupted (XXR); oxidation of even one Trp made peptide inactive. peptide retained activity after acetylation. succinylated DV41 was inactive; the peptide lost activity only when all the three tyrosines are nitrated (Bhugaloo-Vial et al., 1999). Structure: CD studies suggest that the peptide is primarily unordered in phosphate butter, in DPC, or in 80% TFE. Updated 3/2014; 9/2021
Bio-Activity Profile
Antimicrobial
PaperDivercin V41, a new bacteriocin with two disulfide bonds produced by Carnobacterium divergens V41: primary structure and genetic organization
RECORD: Rec_0337992 VERIFIED: YES
Provenance & Taxonomy
Carnobacterium divergens [Bacterium]
Bacteriocin
Structure & Mods
topology not specified [Not included yet]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
PaperPubMed PMID: 9802025 PMID9802025 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/9802025/
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