The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G. Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form part of the ribosomal stalk (called L8). The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion. Acetylation of Ser-2 converts L12 to L7. Lys-82 was found to be 50% monomethylated. Non-methylated. Isolated L10(L12)4. L7, acetylated Ser-2. L12, unacetylated. Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10. Belongs to the bacterial ribosomal protein bL12 family.