Regulation of gene expression on a post-transcriptional level by small non-coding regulatory RNAs (sRNAs) is very common in bacteria. sRNAs base pair with sequences in their target messenger RNAs (mRNAs) and thereby regulate translation initiation or mRNA stability. Specialized RNA-binding proteins (RBPs) facilitate these regulatory sRNA/mRNA interactions by acting as RNA chaperones. A well-known example for such an RNA chaperone which is widespread in bacteria is the Hfq protein. Recently， the ProQ/FinO protein family was identified as a new class of RNA chaperones involved in sRNA based regulation. Only a few members of this protein family have been structurally characterized so far. In particular， the structural basis for RNA-binding and recognition has not yet been established for this class of proteins. Here， we report the H， C and N NMR resonance assignments for a ProQ homolog (Lpp 1663) from the gram-negative pathogenic bacterium Legionella pneumophila which will facilitate further structural and dynamic studies of this protein and its interaction with RNA targets.