The transport of L-methionine by the gram-positive species Brevibacterium linens CNRZ 918 is described. The one transport system (Km = 55 ,uM) found is constitutive for L-methionine, stereospecific, and pH and temperature dependent. Entry of L-methionine into cells is controlled by the internal methionine pool. Competition studies indicate that L-methionine and aL-aminobutyric acid share a common carrier for their transport. Neither methionine derivatives substituted on the amino or carboxyl groups nor D-methionine was an inhibitor, whereas powerful inhibition was shown by L-cysteine, s-methyl-L-cysteine, DL-selenomethionine and DL-homocysteine. Sodium plays important and varied roles in L-methionine transport by B. linens CNRZ 918: (i) it stimulates transport without affecting the Km, (ii) it increases the specific activity (on a biomass basis) of the L-methionine transport system when present with methionine in the medium, suggesting a coinduction mechanism. L-Methionine transport requires an exogenous energy source, which may be succinic, lactic, acetic, or pyruvic acid but not glucose or sucrose. The fact that L-methionine transport was stimulated by potassium arsenate and to a lesser extent by potassium fluoride suggests that high-energy phosphorylated intermediates are not involved in the process. Monensin eliminates stimulation by sodium. Gramicidin and carbonyl cyanide-m-chlorophenylhydrazone act in the presence or absence of Na+. N-Ethylmaleimide, p-chloromercurobenzoate, valinomycin, sodium azide, and potassium cyanide have no or only a partial inhibitory effect. These results tend to indicate that the proton motive force reinforced by the Na+ gradient is involved in the mechanism of energy coupling of L-methionine transport by B. linens CNRZ 918. Thus, this transport is partially similar to the well-described systems in gram-negative bacteria, except for the role of sodium, which is very effective in B. linens, a species adapted to the high sodium levels of its niche.