Sortase B (SrtB)

Sortase B is a membrane-anchored enzyme (~246 amino acids) present in numerous Gram-positive bacterial species, including *Staphylococcus*, *Bacillus*, *Listeria*, and *Clostridium*. It catalyzes the transpeptidation reaction required to covalently link surface proteins—particularly those with the NPQTN sorting motif—to the peptidoglycan layer near the cell membrane. Its major function is to facilitate the acquisition of heme-iron by anchoring iron-scavenging proteins, essential for bacterial survival and pathogenicity during infection. It is structurally characterized by an eight-stranded β-barrel core and a distinctive β6/β7 loop that dictates substrate specificity. Disruption of Sortase B impairs iron uptake and can attenuate the virulence of pathogenic bacteria, making it a promising target for anti-infective therapies. No clinically approved drugs target Sortase B as of now, but inhibition has shown potential in preclinical studies.

Other names

sortase class BSrtBclass B sortase

Inhibition of Sortase B blocks anchoring of iron-scavenging proteins, hindering bacterial iron acquisition and reducing virulence