Large ribosomal subunit assembly factor BipA

UniProtKB accession:  P0DTT0

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UniProtKB description:  A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity, required for 50S subunit assembly at low temperatures, may also play a role in translation (PubMed:30305394). Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable) (PubMed:25777676, PubMed:30305394). Involved in incorporation of ribosomal protein uL6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides (PubMed:30305394). Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleotide binding (PubMed:26163516, PubMed:26283392). Interacts with ribosomes (Ref.12, PubMed:26283392). Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA. Ribosome binding alters its conformation (PubMed:26283392). Genetically its function does not overlap LepA, and it acts in a different pathway during ribosome assembly than does RNA helicase DeaD (PubMed:25777676). GTPase that affects interactions between enteropathogenic E.coli (EPEC) and epithelial cells (PubMed:9622352). Probably regulates expression of proteins required for (at least) K5 polysaccharide production (PubMed:10781541) (Probable). Deletion mutants of bipA are suppressed by an rluC deletion, which no longer modifies uracils 955, 2504 and 2580 to pseudouridine in 23S rRNA; there are 5 other pseudouridine synthases in E.coli, only rluC suppresses this phenotype. Mutating 23S rRNA so the 3 uracils are other nucleotides also suppresses the bipA deletion; pseudouridine-2504 is required for ribosome assembly and translational accuracy (PubMed:18820021, PubMed:25777676).