2‐Cys peroxiredoxins constitute a family of enzymes which catalyze the transfer of electrons from sulfhydryl residues to peroxides and are ubiquitously distributed among all organisms. This paper characterizes the higher plant 2‐Cys‐peroxiredoxin BAS1. (i) Escherichia coli over‐expressing BAS1 exhibit increased tolerance for alkyl hydroperoxides in vivo. This result substantiates the peroxiredoxin function of BAS1. (ii) BAS1 protein is associated with the soluble chloroplast fraction of mesophyll protoplasts. Import and processing of in vitro‐transcribed and cell‐free translated BAS1 protein into isolated chloroplasts provides conclusive evidence that the plant‐specific N‐terminal extension of bas1 encodes the chloroplast import signal which targets the pre‐form of BAS1 to the chloroplast stroma where it is cleaved to its mature size. (iii) Genomic analysis reveals that the targeting signal is encoded by a separate exon in Arabidopsis thaliana. (iv) The amino acid sequence of the BAS1 core protein of higher plants has a higher degree of similarity to open reading frames in the genome of the bluegreen algae Synechochystis PCC sp. 6803 and in the plastome of the red algae Porphyra purpurea than to any other nuclear‐encoded 2‐Cys peroxiredoxin. Therefore, it is tempting to speculate that the chloroplast import signal was added to an ancestor gene of endosymbiotic origin in the course of plant evolution. (v) The bas1 gene expression is regulated under the control of the cellular redox state which is in accordance with the anti‐oxidant function of the enzyme. While oxidative stressors increased expression only slightly, antioxidants such as reduced thiols strongly suppressed the transcript level. The implications of these findings are discussed with respect to the possible physiological functions of BAS1.