Paper Report for: Kok_1994_Biochim.Biophys.Acta_1219_601

Downstream of the Acinetobacter calcoaceticus estA gene, encoding a cell-bound esterase, an open reading frame (orf) was identified, which may encode a protein with a mass of 20.4 kDa. This protein shows extensive similarity to both prokaryotic and eukaryotic peptidyl-prolyl cis-trans isomerases (PPIases) of the cyclophilin sub-class, especially to the periplasmic rotamase (RotA) of Escherichia coli. A putative signal sequence suggests that the product of the Acinetobacter gene, we termed rotA, is located outside the cytoplasm. Transcription of the gene is initiated from a promoter, just upstream of the rotA orf. The observation that two A. calcoaceticus rotA deletion mutants display no apparent mutant phenotype, suggests that this PPIase is not essential for growth of the organism. These mutants, to our knowledge, are the first prokaryotic PPIase mutants reported.