Genomic loci for this biosynthetic pathway

Cluster Type From To
The following clusters are from record BGC0001230.1:
Cluster 1NRP / Polyketide148213

BGC0001230, salinamides biosynthetic gene cluster from Streptomyces sp. CNB091. Locus 1. Full MIBiG entry.

Chemical compounds

Compound: Salinamide A
ChemSpider ID: 8828951
SMILES string: Copy to clipboard
Molecular formula:
Average molecular mass: Da
Molecular activity: Antibacterial
Molecular target: Bacterial RNA polymerase

Class-specific details

Biosynthetic class(es):
NRP / Polyketide
Cyclic depsipeptide (cyclic)
Thioesterase type:
Type I
Release / cyclization type:
Macrolactonization

Nonribosomal peptide synthetases:
sln14
Module 2
A specificity: Threonine
Evidence for specificity: Sequence-based prediction
C domain subtype: Other
sln8
Module 3
A specificity: Valine
Evidence for specificity: Sequence-based prediction
AA is epimerized
C domain subtype: LCL
sln7
Module 4
A specificity: Hydroxyphenylglycine
Evidence for specificity: Sequence-based prediction
C domain subtype: DCL
Module 5
A specificity: Phenylalanine
Evidence for specificity: Sequence-based prediction
C domain subtype: LCL
Scaffold-modifying domain: Methylation
Module 6
A specificity: Threonine
Evidence for specificity: Sequence-based prediction
AA is epimerized
C domain subtype: LCL
sln6
Module 7
A specificity: Serine
Evidence for specificity: Sequence-based prediction
C domain subtype: DCL
sln9
Module 8
A specificity: Glycine
Evidence for specificity: Sequence-based prediction
C domain subtype: Other
Polyketide subclass:
Macrolide (linear)
Polyketide synthase subclass:
Modular type I
Starter unit:
Isobutyryl-CoA
Thioesterase type:
None
Release / cyclization type:
Other

Modular polyketide synthases:
sln14
Module 0
AT specificity: Isobutyryl-CoA
Evidence for specificity: Sequence-based prediction
Scaffold-modifying domain: None
Module 1
AT specificity: Methylmalonyl-CoA
Evidence for specificity: Sequence-based prediction
KR stereochemistry: L-OH
Scaffold-modifying domain: None

Gene cluster description

salinamides (BGC0001230). Gene Cluster 1. Biosynthetic class = NRP/Polyketide. GenBank BK009377, positions 1796-44697. Click on genes for more information.

Legend:

biosynthetic genes
transport-related genes
regulatory genes
other genes

Domain annotation

Homologous known gene clusters

General MIBiG information on this cluster

Complete gene cluster sequence?complete
Evidence for cluster-compound connection:Knock-out studies, Enzymatic assays, Heterologous expression, Sequence-based prediction
MIxS-compliance:Unknown
Comments:You can also contact Lauren Ray (laray@ucsd.edu) with regards to this MIBiG submission.
Contact for this cluster:Bradley Moore (Scripps Institution of Oceanography, University of California San Diego)

Literature references

1. Hassan HM et al. (2015) Salinamide F, new depsipeptide antibiotic and inhibitor of bacterial RNA polymerase from a marine-derived Streptomyces sp. J Antibiot (Tokyo) 68(3):206-9. doi: 10.1038/ja.2014.122. Epub 2014 Sep
2. Degen D et al. (2014) Transcription inhibition by the depsipeptide antibiotic salinamide A. Elife 3:e02451. doi: 10.7554/eLife.02451.
3. Tan L, Ma D. (2008 TI) Total synthesis of salinamide A: a potent anti-inflammatory bicyclic depsipeptide. Angew Chem Int Ed Engl 47(19):3614-7. doi: 10.1002/anie.200800397.
4. Bradley S. Moore, Dieter Seng. (1998) Biosynthesis of the bicyclic depsipeptide salinamide A in Streptomyces sp. CNB-091: Origin of the carbons. Tetrahedron Letters, vol. 39, no. 23, pp. 3915-3918
5. Bradley S. Moore, Jacqueline A. Trischman, Dieter Seng, David Kho, Paul R. Jensen, William Fenical. (1999) Salinamides, Antiinflammatory Depsipeptides from a Marine Streptomycete. The Journal of Organic Chemistry, vol. 64, no. 4, pp. 1145-1150
6. Jacqueline A. Trischman, Dianne M. Tapiolas, Paul R. Jensen, Ryan Dwight, William Fenical, Tawnya C. McKee, Chris M. Ireland, Thomas J. Stout, Jon Clardy. (1994) Salinamides A and B: anti-inflammatory depsipeptides from a marine streptomycete. Journal of the American Chemical Society, vol. 116, no. 2, pp. 757-758