dbacp03708
General Description
Peptide name : Laterosporulin10
Source/Organism : Spore-forming, rod-shaped bacterium strain SKDU10
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : ACVNQCPDAIDRFIVKDKGCHGVEKKYYKQVYVACMNGQHLYCRTEWGGPCQL
Peptide length: 53
C-terminal modification: Not found
N-terminal modification : Not found
Non-natural peptide information: None
Activity Information
Assay type : Not specified
Assay time : Not found
Activity : Not found
Cell line : Not found
Cancer type : Not found
Other activity : Anti-microbial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 6067.9788 Dalton
Aliphatic index : 0.624
Instability index : 27.3415
Hydrophobicity (GRAVY) : -0.428
Isoelectric point : 8.2995
Charge (pH 7) : 1.9108
Aromaticity : 0.113
Molar extinction coefficient (cysteine, cystine): (11460, 11835)
Hydrophobic/hydrophilic ratio : 1.12
hydrophobic moment : -0.356
Missing amino acid : S
Most occurring amino acid : C
Most occurring amino acid frequency : 6
Least occurring amino acid : F
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.2, 0.3)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](C)N)C(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)O)C(C)C)C(C)C)C(C)C)C(C)C)[C@@H](C)CC
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | EEETTCCCCHHHHHHTTTTTTTHHHHHTTEEEEEEETTTCEEEEETTTCCCEE |
| Chou-Fasman (CF) | EEECCCCCCEEEEECCCCCCHHHHEEEEEEEECCCCCCEEEECCCCCCCCCCC |
| Neural Network (NN) | CCCCCCCCCCCHHHHCCCCCCCCCCCCCCCEEEEHHCCCCCECCCCCCCCCCC |
| Joint/Consensus | EEECCCCCCCCHHHHCCCCCCCCCCCCCCEEEEECCCCCCEECCCCCCCCCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
CancerPPD : Not available
ApIAPDB : Not available
CancerPPD2 ID : Not available
Reference
1 : Baindara P, et al. Laterosporulin10: a novel defensin like Class IId bacteriocin from Brevibacillus sp. strain SKDU10 with inhibitory activity against microbial pathogens. Microbiology (Reading). 2016; 162:1286-1299. doi: 10.1099/mic.0.000316
Literature
Paper title : Laterosporulin10: a novel defensin like Class IId bacteriocin from Brevibacillus sp. strain SKDU10 with inhibitory activity against microbial pathogens.
Doi : https://doi.org/10.1099/mic.0.000316
Abstract : Bacteriocins are antimicrobial peptides (AMPs) produced by bacteria to acquire survival benefits during competitive inter- and intra-species interactions in complex ecosystems. In this study, an AMP-producing soil bacterial strain designated SKDU10 was isolated and identified as a member of the genus Brevibacillus. The AMP produced by strain SKDU10 identified as a class IId bacteriocin with 57.6 % homology to laterosporulin, a defensin-like class IId bacteriocin. However, substantial differences were observed in the antimicrobial activity spectrum of this bacteriocin named laterosporulin10 when compared to laterosporulin. Laterosporulin10 effectively inhibited the growth of Staphylococcus aureus and Mycobacterium tuberculosis (Mtb H37Rv) with LD50 values of 4.0 µM and 0.5 µM, respectively. Furthermore, laterosporulin10 inhibited the growth of Mtb H37Rv strain at about 20 times lower MIC value compared to S. aureus MTCC 1430 or M. smegmatis MC2 155 in vitro and ex vivo. Electron micrographs along with membrane permeabilization studies using FACS analysis revealed that laterosporulin10 is a membrane-permeabilizing peptide. Interestingly, laterosporulin10 was able to efficiently kill Mtb H37Rv strain residing inside the macrophages and did not show haemolysis up to 40 µM concentration.