Abstract
YveA of Bacillus subtilis, a putative transporter of the amino acid/polyamine/organocation (APC) superfamily, is shown to mediate uptake of both L-aspartate and L-glutamate as well as having sensitivity to L-aspartate hydroxamate. This 14 TMS protein is the primary aspartate uptake system in B. subtilis and serves as the prototype for a new family within the APC superfamily.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Transport Systems, Acidic / genetics*
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Amino Acid Transport Systems, Acidic / metabolism
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Amino Acids / metabolism
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Asparagine / analogs & derivatives*
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Asparagine / pharmacology
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Aspartic Acid / metabolism*
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Bacillus subtilis / drug effects
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Bacillus subtilis / genetics*
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Bacillus subtilis / metabolism
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cell Division / physiology
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Cloning, Molecular
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Glutamic Acid / metabolism
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Mutation
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Phylogeny
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Substrate Specificity
Substances
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Amino Acid Transport Systems, Acidic
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Amino Acids
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Bacterial Proteins
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Carrier Proteins
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Recombinant Fusion Proteins
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YveA protein, Bacillus subtilis
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beta-aspartylhydroxamic acid
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Aspartic Acid
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Glutamic Acid
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Asparagine