Identification and characterization of xcpR encoding a subunit of the general secretory pathway necessary for dodecane degradation in Acinetobacter calcoaceticus ADP1.

A mutant of Acinetobacter calcoaceticus ADP1 unable to grow on alkanes was complemented for growth on hexadecane with a DNA fragment encoding a protein with homology to XcpR, a subunit of the general secretion pathway for exoproteins in Pseudomonas aeruginosa. Insertional inactivation of xcpR in A. calcoaceticus ADP1 by transcriptional fusion to lacZ abolishes secretion of lipase and esterase and leads to lack of growth on dodecane and slower growth on hexadecane. We, therefore, propose the participation of a secreted protein in alkane degradation.