Subtilosin_A | |||||||||
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structure of Subtilosin A
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Identifiers | |||||||||
Symbol | Subtilosin_A | ||||||||
Pfam | PF11420 | ||||||||
InterPro | IPR021539 | ||||||||
TCDB | 1.C.84 | ||||||||
OPM superfamily | 508 | ||||||||
OPM protein | 1pxq | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Microcins are very small bacteriocins, composed of a relatively few peptides. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of E. coli. Subtilosin A is another bacteriocin from Bacillus subtilis. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22,Thr28 and Phe31.
It is found that these bacteriocins target and eliminate iron-starved pathogens, which is found specifically in an inflamed gut where the E. Coli strain prefer to thrive. Specifically, the protein targets the pathogens are producing iron-scavenging protein in response to a low iron environment. Researchers found. E. coli Nissle’s microcins killed diarrhea-inducing bacteria called Salmonella Enterica in the guts of infected mice. Microcins also helped Nissle outcompete a different, more virulent of E. coli found in the infected mice's guts.
BACTIBASE database is an open-access database for bacteriocins including microcins.