UniProt functional annotation for P0A7W1



	UniProt functional annotation for P0A7W1

UniProt codes: P0A7W1, P02356.

Organism: Escherichia coli (strain K12).

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

Function: With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). {ECO:0000269|PubMed:15652481}.

Function: Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. {ECO:0000269|PubMed:15652481}.

Function: The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. {ECO:0000269|PubMed:15652481}.

Subunit: Part of the 30S ribosomal subunit (PubMed:363452, PubMed:4273819, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts proteins S4 and S8. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity (PubMed:15652481). Can be cross-linked to mRNA (PubMed:1712292). {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:15652481, ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:1712292, ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875, ECO:0000269|PubMed:363452, ECO:0000269|PubMed:4273819}.

Domain: The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.

Mass spectrometry: Mass=17514.8; Method=MALDI; Evidence={ECO:0000269|PubMed:10094780};

Miscellaneous: Altered S5 proteins have been identified in a number of mutants. Some mutations in S5 have been shown to increase translational error frequencies.

Miscellaneous: Some mutants in this protein can partially suppress an alanyl-tRNA synthetase mutant.

Similarity: Belongs to the universal ribosomal protein uS5 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


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



Function:		With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). {ECO:0000269\|PubMed:15652481}.



Function:		Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. {ECO:0000269\|PubMed:15652481}.



Function:		The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. {ECO:0000269\|PubMed:15652481}.


Subunit:		Part of the 30S ribosomal subunit (PubMed:363452, PubMed:4273819, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts proteins S4 and S8. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity (PubMed:15652481). Can be cross-linked to mRNA (PubMed:1712292). {ECO:0000269\|PubMed:10094780, ECO:0000269\|PubMed:12244297, ECO:0000269\|PubMed:12809609, ECO:0000269\|PubMed:15652481, ECO:0000269\|PubMed:16272117, ECO:0000269\|PubMed:1712292, ECO:0000269\|PubMed:27906160, ECO:0000269\|PubMed:27906161, ECO:0000269\|PubMed:27934701, ECO:0000269\|PubMed:28077875, ECO:0000269\|PubMed:363452, ECO:0000269\|PubMed:4273819}.
Domain:		The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Mass spectrometry:		Mass=17514.8; Method=MALDI; Evidence={ECO:0000269\|PubMed:10094780};
Miscellaneous:		Altered S5 proteins have been identified in a number of mutants. Some mutations in S5 have been shown to increase translational error frequencies.
Miscellaneous:		Some mutants in this protein can partially suppress an alanyl-tRNA synthetase mutant.
Similarity:		Belongs to the universal ribosomal protein uS5 family. {ECO:0000305}.