P37547 · RNM5_BACSU
- ProteinRibonuclease M5
- GenernmV
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids186 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. Releases 5'-phosphoryl and 3'-hydroxy termini.
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Note: Divalent metal cations; Mg2+ > Mn2+ > Ca2+.
pH Dependence
Optimum pH is 7-8.5 at 37 degrees Celsius.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | metal ion binding | |
Molecular Function | ribonuclease M5 activity | |
Molecular Function | rRNA binding | |
Biological Process | ribosome biogenesis | |
Biological Process | rRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease M5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP37547
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with 70S ribosomes.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Not essential. Accumulation of precursor forms of 5S rRNA in total, ribosomes and polysome RNA preparations; smaller forms (126 and 135 nucleotides) are predominantly found in ribosomes and polysomes. Each of the 10 rrn operons gives rise to a different 5S rRNA precursor due to differences in their 3' ends.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 10 | Loss of activity, 50% rRNA-binding. | ||||
Sequence: E → A | ||||||
Mutagenesis | 11 | 30-fold loss of activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 31 | Loss of activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 56 | Loss of activity, rRNA-binding normal. | ||||
Sequence: D → A | ||||||
Mutagenesis | 58 | Loss of activity, rRNA-binding normal. | ||||
Sequence: D → A | ||||||
Mutagenesis | 61 | Loss of activity in vivo, about 100-fold loss in vitro. | ||||
Sequence: G → A | ||||||
Mutagenesis | 65 | 100-fold loss of activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 107 | 10-fold loss of activity. | ||||
Sequence: L → A | ||||||
Mutagenesis | 140-142 | Loss of activity, significant loss of rRNA binding. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000049440 | 1-186 | Ribonuclease M5 | |||
Sequence: MKIKEIIVVEGRDDTARIKLAVDADTIETNGSAIDDHVIDQIRLAQKTRGVIILTDPDFPGEKIRKTISEAVPGCKHAFLPKHLAKPKNKRGIGVEHASVESIRACLENVHEEMEAQPSDISAEDLIHAGLIGGPAAKCRRERLGDLLKIGYTNGKQLQKRLQMFQIKKSDFMSALDTVMREEQNE |
Proteomic databases
Interaction
Subunit
Requires ribosomal protein L18 (rplR) for catalysis; it can be replaced by 30% dimethylsulfoxide suggesting L18 functions as an rRNA folding chaperone.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-94 | Toprim | ||||
Sequence: KEIIVVEGRDDTARIKLAVDADTIETNGSAIDDHVIDQIRLAQKTRGVIILTDPDFPGEKIRKTISEAVPGCKHAFLPKHLAKPKNKRGIG |
Sequence similarities
Belongs to the ribonuclease M5 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length186
- Mass (Da)20,674
- Last updated1994-10-01 v1
- ChecksumCE18BC3D9F9C2F81
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D26185 EMBL· GenBank· DDBJ | BAA05276.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB11817.1 EMBL· GenBank· DDBJ | Genomic DNA |