In several types of bacteria, the Kdp ATPase (comprising of the KdpABC complex) is an inducible, high-affinity potassium transporter that scavenges K ؉ from the environment. The cyanobacterium Anabaena sp. strain L-31 showed the presence of not one but two distinct kdp operons in its genome. The kdp1 consisted of kdpA1B1G1C1D genes, whereas the kdp2 contained the kdpA2B2G2C2 genes. Among the regulatory genes, the kdpD open reading frame of Anabaena sp. strain L-31 was truncated compared to the kdpD of other bacteria, whereas a kdpE-like gene was absent in the vicinity of the two kdp operons. In response to K ؉ limitation (<0.05 mM external K ؉ ), only kdp2 (and not kdp1) expression could be detected as a 5.3-kb transcript on Northern blots, indicating that kdpA2B2G2C2 genes constitute a polycystronic operon. Unlike E. coli, addition of osmolytes like NaCl, or a change in pH of the medium did not enhance the kdp expression in Anabaena sp. strain L-31. Interestingly, the Anabaena sp. strain L-31 kdp2 operon was strongly induced in response to desiccation stress. The addition of K ؉ to K ؉ -starved cultures resulted in repression and degradation of kdp2 transcripts. Our results clearly show that kdp2 is the major kdp operon expressed in Anabaena sp. strain L-31 and may play an important role in adaptation to K ؉ limitation and desiccation stress.Potassium, the major intracellular cation in bacteria, is involved in various physiological processes such as turgor adaptation (15), activation of cellular enzymes (29), and pH homeostasis (12). In nitrogen-fixing cyanobacteria such as Anabaena spp., K ϩ also regulates gene expression and vital metabolic processes such as photosynthesis and nitrogen fixation (1, 2). Despite very low levels of K ϩ available in most environments (0.1 to 10 mM), the bacteria maintain a very high concentration of K ϩ (0.2 to 0.6 M) within their cells and have evolved several distinct K ϩ uptake and efflux systems to regulate their internal K ϩ concentration (15). In Escherichia coli the constitutively expressed TrkG, TrkH, and Kup uptake systems have a low affinity for K ϩ but are competent to maintain the required levels K ϩ under normal physiological conditions (20). Under conditions of severe K ϩ limitation or osmotic upshift or when the low-affinity transporters are unable to meet the cell's demand for K ϩ , the high-affinity KdpATPase (K ϩ -dependent ATPase) is expressed (4). The K m of E. coli KdpATPase for K ϩ is 2 M and the cells expressing Kdp can reduce the K ϩ concentration in the medium to as low as 50 nM (28).Earlier studies had shown the kdp homologs to be widely distributed among the gram-negative bacteria (32). Genome sequencing has now shown kdp homologs to be present also in cyanobacteria, gram-positive bacteria, and the Archaea. We have previously demonstrated the presence of KdpB-like polypeptide in three different strains of the nitrogen-fixing cyanobacteria Anabaena spp. (6). The KdpB was induced under conditions of K ϩ limitation, and the KdpB protein was shown to be loc...