UniProt functional annotation for P0ADY3



	UniProt functional annotation for P0ADY3

UniProt codes: P0ADY3, P02411.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117). {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:22829778}.

Function: Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation. {ECO:0000269|PubMed:22829778}.

Subunit: Part of the 50S ribosomal subunit (PubMed:352727, PubMed:7556101, PubMed:2665813, PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts L19 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association. {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:10756104, ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:151587, ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:24844575, ECO:0000269|PubMed:25310980, ECO:0000269|PubMed:2665813, ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:352727, ECO:0000269|PubMed:7556101}.

Mass spectrometry: Mass=13540.2; Method=MALDI; Evidence={ECO:0000269|PubMed:10094780};

Similarity: Belongs to the universal ribosomal protein uL14 family. {ECO:0000255|HAMAP-Rule:MF_01367}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117). {ECO:0000269\|PubMed:12809609, ECO:0000269\|PubMed:16272117, ECO:0000269\|PubMed:22829778}.



Function:		Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation. {ECO:0000269\|PubMed:22829778}.


Subunit:		Part of the 50S ribosomal subunit (PubMed:352727, PubMed:7556101, PubMed:2665813, PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts L19 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association. {ECO:0000269\|PubMed:10094780, ECO:0000269\|PubMed:10756104, ECO:0000269\|PubMed:12809609, ECO:0000269\|PubMed:151587, ECO:0000269\|PubMed:16272117, ECO:0000269\|PubMed:24844575, ECO:0000269\|PubMed:25310980, ECO:0000269\|PubMed:2665813, ECO:0000269\|PubMed:27906160, ECO:0000269\|PubMed:27906161, ECO:0000269\|PubMed:352727, ECO:0000269\|PubMed:7556101}.
Mass spectrometry:		Mass=13540.2; Method=MALDI; Evidence={ECO:0000269\|PubMed:10094780};
Similarity:		Belongs to the universal ribosomal protein uL14 family. {ECO:0000255\|HAMAP-Rule:MF_01367}.