Acinetobacter baumannii is a Gram-negative opportunistic nosocomial pathogen that causes pneumonia, soft-tissue and systemic infections. Screening of a transposon insertion library of A. baumannii ATCC 19606(T) resulted in the identification of the 2010 derivative, which although capable of growing well in iron-rich media, failed to prosper under iron chelation. Genetic, molecular and functional assays showed that 2010's iron-utilization deficient phenotype is due to an insertion within the 3' -end of secA, which results in the production of a C-terminal truncated derivative of SecA. SecA plays a critical role in protein translocation through the SecYEG membrane channel. Accordingly, the secA mutation resulted in undetectable amounts of the ferric-acinetobactin outer membrane receptor protein BauA, while not affecting the production of other acinetobactin membrane protein transport components, such as BauB and BauE, or the secretion of acinetobactin by 2010 cells cultured in the presence of sub-inhibitory concentrations of the synthetic iron chelator 2,2' -dipyridyl. Outer membrane proteins involved in nutrient transport, adherence and biofilm formation were also reduced in 2010. The SecA truncation also increased production of 30 different proteins, including proteins involved in adaptation/tolerance responses. Although some of these protein changes could negatively affect the pathobiology of the 2010 derivative, its virulence defect is mainly due to its inability to acquire iron via the acinetobactin-mediated system. These results together indicate that although the C-terminus of the A. baumannii ATCC 19606(T) SecA is not essential for viability, it plays a critical role in the production and translocation of different proteins and virulence.
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