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The Methionine ABC transporter, commonly referred to as the MetNIQ or MetD system, is a high-affinity nutrient uptake complex found in a wide range of bacteria, including Escherichia coli, Streptococcus pneumoniae, and Neisseria species. It is composed of three essential subunits: the ATPase MetN, the transmembrane permease MetI, and the substrate-binding protein MetQ. This system is responsible for the energy-dependent transport of L- and D-methionine from the extracellular environment into the bacterial cytoplasm, where it supports critical functions such as protein synthesis, S-adenosylmethionine (SAM) production, and bacterial virulence. In human pathogens like Neisseria gonorrhoeae, the surface-exposed MetQ protein is a major vaccine candidate due to its high conservation and ability to elicit protective immune responses. While the bacterial system is a target for novel antibacterials, the human functional equivalent is the L-type amino acid transporter 1 (LAT1/SLC7A5), which is a significant therapeutic target in oncology. Cancer cells often exhibit methionine addiction, and inhibitors like JPH203 (Nanvuranlat) are being developed to disrupt methionine uptake and suppress tumor growth.
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