UniProt functional annotation for P28619



	UniProt functional annotation for P28619

UniProt code: P28619.

Organism: Bacillus subtilis (strain 168).

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.

Function: Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. Plays a role in the secondary pathway of 23S rRNA 3' end maturation (PubMed:19880604). {ECO:0000255|HAMAP-Rule:MF_00564, ECO:0000269|PubMed:19880604}.

Catalytic activity: Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:11132, Rhea:RHEA- COMP:11133, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:83401; EC=2.7.7.56; Evidence={ECO:0000255|HAMAP-Rule:MF_00564};

Subunit: Homohexameric ring arranged as a trimer of dimers (PubMed:14767080). It has been suggested that the active form is the dimer which binds tRNA and that the hexameric form protects the substrate recognition loop (approximately residues 65-82) from proteolysis (PubMed:14767080). {ECO:0000255|HAMAP-Rule:MF_00564, ECO:0000269|PubMed:14767080}.

Disruption phenotype: Correct processing of the 3' end of 23S rRNA no longer occurs in the absence of mrnC. {ECO:0000269|PubMed:19880604}.

Miscellaneous: Sulfate ions in the crystal structure may represent the inorganic phosphate substrate. {ECO:0000305|PubMed:14767080}.

Similarity: Belongs to the RNase PH family. {ECO:0000255|HAMAP- Rule:MF_00564}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus subtilis (strain 168).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.



Function:		Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. Plays a role in the secondary pathway of 23S rRNA 3' end maturation (PubMed:19880604). {ECO:0000255\|HAMAP-Rule:MF_00564, ECO:0000269\|PubMed:19880604}.


Catalytic activity:		Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate + tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:11132, Rhea:RHEA- COMP:11133, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:83401; EC=2.7.7.56; Evidence={ECO:0000255\|HAMAP-Rule:MF_00564};
Subunit:		Homohexameric ring arranged as a trimer of dimers (PubMed:14767080). It has been suggested that the active form is the dimer which binds tRNA and that the hexameric form protects the substrate recognition loop (approximately residues 65-82) from proteolysis (PubMed:14767080). {ECO:0000255\|HAMAP-Rule:MF_00564, ECO:0000269\|PubMed:14767080}.
Disruption phenotype:		Correct processing of the 3' end of 23S rRNA no longer occurs in the absence of mrnC. {ECO:0000269\|PubMed:19880604}.
Miscellaneous:		Sulfate ions in the crystal structure may represent the inorganic phosphate substrate. {ECO:0000305\|PubMed:14767080}.
Similarity:		Belongs to the RNase PH family. {ECO:0000255\|HAMAP- Rule:MF_00564}.