A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation. Forms a complex with KhpA which presumably binds to about 170 cellular RNAs (mRNA, tRNA intergenic RNA and sRNAs); the proteins alone each bind the same set of RNAs. Suppresses the requirement for PBP2b (penA, a transpeptidase) in peripheral peptidogylcan (PG) synthesis (PubMed:28941257). May function as a pleiotropic RNA chaperone controlling pneumococcal cell division, including PG homeostasis and regulating peripheral PG synthesis by the elongasome (Probable). Interacts with KhpA; the 2 proteins colocalize throughout the cell cycle, with some increase at midcell in dividing cells (PubMed:28941257). Interacts with StkP which phosphorylates it, interacts with MltG, MreC, RodZ and YidC2 (By similarity). Some protein localizes to midcell in the septal area, the rest remains in the cytoplasm. Has an N-terminal Jag-N domain, a linker with a phosphorylated Thr, and 2 RNA-binding domains (KH and R3H). Phosphorylated on Thr-89 by StkP; there is another poorly phosphorylated residue in the protein. Dephosphorylated by PhpP. Suppresses a pbp2b (penA) deletion, grows slowly and is smaller than wild-type; about 50% of the volume of wild-type cells. Increased accumulation of FtsA and FtsZ protein. Significant up-regulation of genes of the WalRK regulon. Also partially suppresses deletions in other genes involved in peripheral PG synthesis; gpsB, mreCD, rodA and rodZ but not mltG. Slight decrease in net phosphorylation (by StpK/PhpP) of DivIA and MapZ/StpK. Double khpA-khpB deletions have the same phenotypes. Belongs to the KhpB RNA-binding protein family.