Literature summary for 3.4.21.89 extracted from

Steed, D.B.; Liu, J.; Wasbrough, E.; Miller, L.; Halasohoris, S.; Miller, J.; Somerville, B.; Hershfield, J.R.; Romesberg, F.E.
Origins of Yersinia pestis sensitivity to the arylomycin antibiotics and the inhibition of type I signal peptidase (2015), Antimicrob. Agents Chemother., 59, 3887-3898 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene lepB, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)	Yersinia pestis

Protein Variants

Protein Variants	Comment	Organism
P91S	construction of LepB(P91S) mutant strain DBS600 via allelic exchange and site-directed mutagenesis to introduce the point mutation. The mutant can be complemented by expression of wild-type SPase from Yersinia pestis or Escherichia coli	Yersinia pestis

Inhibitors

Inhibitors	Comment	Organism	Structure
arylomycin A-C16	Yersinia pestis strain KIM6+, unlike most Enterobacteriaceae, is susceptible to the arylomycins, a class of natural-product lipopeptide antibiotics that inhibit signal peptidase I (SPase). The arylomycin activity is conserved against a broad range of Yersinia pestis strains, overview. Alterations to each component of the Yersinia pestis lipopolysaccharide (O antigen, core, and lipid A) make at most only a small contribution to the unique sensitivity against arylomycin, also an increased affinity of the Yersinia pestis SPase for the antibiotic is not detected. Instead, the origins of the sensitivity can be traced to an increased dependence on SPase activity that results from high levels of protein secretion under physiological conditions. Deletion of the gene encoding the highly expressed cell adhesion protein Ail (locus tag y1324, UniProt ID Q8D0Z7) significantly alleviates sensitivity and overexpression of Ail or Escherichia coli maltose-binding protein then restores sensitivity, the arylomycin susceptibility of Yersinia pestis results from a temperature-dependent increase in protein secretion	Yersinia pestis
Ciprofloxacin	1-cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-ylquinoline-3-carboxylic acid	Yersinia pestis
additional information	strain identifiers and MIC values of arylomycin A-C16 and ciprofloxacin for the 30-member Yersinia pestis panel, overview. The MIC values increase with decreasing temperature	Yersinia pestis

Organism

Organism	UniProt	Comment	Textmining
Yersinia pestis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Yersinia pestis

Synonyms

Synonyms	Comment	Organism
LepB	-	Yersinia pestis
SPase	-	Yersinia pestis
type I signal peptidase	-	Yersinia pestis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Yersinia pestis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Yersinia pestis

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Release 2023.1 (January 2023)