Peptide name : UvrABC system protein A

Source/Organism : Streptomyces lasalocidi

Linear/Cyclic : Linear

Chirality : Not found

Peptide length: 792

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 83988.5113 Dalton

Aliphatic index : 0.924

Instability index : 28.7389

Hydrophobicity (GRAVY) : -0.023

Isoelectric point : 6.1427

Charge (pH 7) : -8.5596

Aromaticity : 0.053

Molar extinction coefficient (cysteine, cystine): (39880, 40505)

Hydrophobic/hydrophilic ratio : 1.20612813

hydrophobic moment : 0.116

Missing amino acid : None

Most occurring amino acid : G

Most occurring amino acid frequency : 85

Least occurring amino acid : W

Least occurring amino acid frequency : 4

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.3)

SMILES Notation: 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1 : Gade P, et al. Structural and functional analyses of the echinomycin resistance conferring protein Ecm16 from Streptomyces lasalocidi. Sci Rep. 2023; 13:7980. doi: 10.1038/s41598-023-34437-9

2 : Watanabe K, et al. Total biosynthesis of antitumor nonribosomal peptides in Escherichia coli. Nat Chem Biol. 2006; 2:423-8. doi: 10.1038/nchembio803

Paper title : Structural and functional analyses of the echinomycin resistance conferring protein Ecm16 from Streptomyces lasalocidi.

Doi : https://doi.org/10.1038/s41598-023-34437-9

Abstract : Echinomycin is a natural product DNA bisintercalator antibiotic. The echinomycin biosynthetic gene cluster in Streptomyces lasalocidi includes a gene encoding the self-resistance protein Ecm16. Here, we present the 2.0 Å resolution crystal structure of Ecm16 bound to adenosine diphosphate. The structure of Ecm16 closely resembles that of UvrA, the DNA damage sensor component of the prokaryotic nucleotide excision repair system, but Ecm16 lacks the UvrB-binding domain and its associated zinc-binding module found in UvrA. Mutagenesis study revealed that the insertion domain of Ecm16 is required for DNA binding. Furthermore, the specific amino acid sequence of the insertion domain allows Ecm16 to distinguish echinomycin-bound DNA from normal DNA and link substrate binding to ATP hydrolysis activity. Expression of ecm16 in the heterologous host Brevibacillus choshinensis conferred resistance against echinomycin and other quinomycin antibiotics, including thiocoraline, quinaldopeptin, and sandramycin. Our study provides new insight into how the producers of DNA bisintercalator antibiotics fend off the toxic compounds that they produce.

Paper title : Total biosynthesis of antitumor nonribosomal peptides in Escherichia coli.

Doi : https://doi.org/10.1038/nchembio803

Abstract : Nonribosomal peptides (NRPs) are a class of microbial secondary metabolites that have a wide variety of medicinally important biological activities, such as antibiotic (vancomycin), immunosuppressive (cyclosporin A), antiviral (luzopeptin A) and antitumor (echinomycin and triostin A) activities. However, many microbes are not amenable to cultivation and require time-consuming empirical optimization of incubation conditions for mass production of desired secondary metabolites for clinical and commercial use. Therefore, a fast, simple system for heterologous production of natural products is much desired. Here we show the first example of the de novo total biosynthesis of biologically active forms of heterologous NRPs in Escherichia coli. Our system can serve not only as an effective and flexible platform for large-scale preparation of natural products from simple carbon and nitrogen sources, but also as a general tool for detailed characterizations and rapid engineering of biosynthetic pathways for microbial syntheses of novel compounds and their analogs.