The psychrophilic model bacterium Pseudoalteromonas haloplanktis is characterized by remarkably fast growth rates under low-temperature conditions in a range from 5°C to 20°C. In this study the proteome of cellular compartments, the cytoplasm and periplasm, of P. haloplanktis strain TAC125 was analyzed under exponential growth conditions at a permissive temperature of 16°C. By means of two-dimensional protein gel electrophoresis and mass spectrometry, a first inventory of the most abundant cytoplasmic and periplasmic proteins expressed in a peptone-supplemented minimal medium was established. By this approach major enzymes of the amino acid catabolism of this marine bacterium could be functionally deduced. The cytoplasmic proteome showed a predominance of amino acid degradation pathways and tricarboxylic acid (TCA) cycle enzymes but also the protein synthesis machinery. Furthermore, high levels of cold acclimation and oxidative stress proteins could be detected at this moderate growth temperature. The periplasmic proteome was characterized by a significant abundance of transporters, especially of highly expressed putative TonB-dependent receptors. This high capacity for protein synthesis, efficient amino acid utilization, and substrate transport may contribute to the fast growth rates of the copiotrophic bacterium P. haloplanktis in its natural environments.The Antarctic marine environment is characterized by low temperatures that very seldom exceed 0°C. Despite the permanent low temperatures, the surface water and the pack ice zones in this region harbor a surprisingly high level of microbial activity. The most abundant bacterial populations in sea ice samples from Antarctic coastal areas belong mainly to four phylogenetic groups: the Gram-positive branch, the Flexibacter-Bacteroides-Cytophaga phylum, and the alpha and gamma subdivisions of the proteobacteria (4). Up to 50% of the identified bacterial isolates could be assigned to the gammaproteobacteria (5). It is assumed that this group of heterotrophic bacteria plays a key role in carbon cycling in this extreme environment.A prominent, cold-adapted member of this group is the obligatory marine bacterium Pseudoalteromonas haloplanktis TAC125, which was isolated from an Antarctic coastal seawater sample (32). P. haloplanktis features remarkable metabolic versatility and has become a model organism of psychrophilic bacteria. Several cold-adapted proteins of this species have been characterized, such as aspartate aminotransferase (2), polynucleotide phosphorylase (18), DNA ligase (25), cytochrome c (15), superoxide dismutase (33), lipase (14), esterases (46), xylanase (10), cellulase (47), and alpha-amylase (21, 43). As expected, most of these enzymes possess strong catalytic activities at lower temperatures and need less activation energy than do their mesophilic or thermophilic counterparts (31). It is worth noting that, quite unexpectedly and presumably associated with the cold salt-washing process, P. haloplanktis has also been found to develop routinely on ...