RNM5_STAA8
ID RNM5_STAA8 Reviewed; 178 AA.
AC Q2G0T1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribonuclease M5 {ECO:0000255|HAMAP-Rule:MF_01469};
DE EC=3.1.26.8 {ECO:0000255|HAMAP-Rule:MF_01469};
DE AltName: Full=RNase M5 {ECO:0000255|HAMAP-Rule:MF_01469};
DE AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000255|HAMAP-Rule:MF_01469};
GN Name=rnmV {ECO:0000255|HAMAP-Rule:MF_01469};
GN OrderedLocusNames=SAOUHSC_00463;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: Required for correct processing of both the 5' and 3' ends of
CC 5S rRNA precursor. Cleaves both sides of a double-stranded region
CC yielding mature 5S rRNA in one step. {ECO:0000255|HAMAP-Rule:MF_01469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 21 and 42
CC nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA
CC precursor.; EC=3.1.26.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01469};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01469};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01469};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01469}.
CC -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000255|HAMAP-
CC Rule:MF_01469}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000253; ABD29618.1; -; Genomic_DNA.
DR RefSeq; WP_000700080.1; NZ_LS483365.1.
DR RefSeq; YP_499042.1; NC_007795.1.
DR AlphaFoldDB; Q2G0T1; -.
DR SMR; Q2G0T1; -.
DR STRING; 1280.SAXN108_0543; -.
DR EnsemblBacteria; ABD29618; ABD29618; SAOUHSC_00463.
DR GeneID; 3920323; -.
DR KEGG; sao:SAOUHSC_00463; -.
DR PATRIC; fig|93061.5.peg.418; -.
DR eggNOG; COG1658; Bacteria.
DR HOGENOM; CLU_109405_0_0_9; -.
DR OMA; RLQMFQI; -.
DR PRO; PR:Q2G0T1; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043822; F:ribonuclease M5 activity; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd01027; TOPRIM_RNase_M5_like; 1.
DR HAMAP; MF_01469; RNase_M5; 1.
DR InterPro; IPR004466; RNase_M5.
DR InterPro; IPR025156; RNase_M5_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034141; TOPRIM_RNase_M5-like.
DR Pfam; PF13331; DUF4093; 1.
DR Pfam; PF01751; Toprim; 1.
DR SMART; SM00493; TOPRIM; 1.
DR TIGRFAMs; TIGR00334; 5S_RNA_mat_M5; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding.
FT CHAIN 1..178
FT /note="Ribonuclease M5"
FT /id="PRO_0000416757"
FT DOMAIN 4..100
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ SEQUENCE 178 AA; 20092 MW; B72AE85FE580E690 CRC64;
MKINEFIVVE GRDDTERVKR AVECDTIETN GSAINEQTLE VIRNAQQSRG VIVLTDPDFP
GDKIRSTITE HVKGVKHAYI DREKAKNKKG KIGVEHADLI DIKEALMHVS SPFDEAYESI
DKSVLIELGL IVGKDARRRR EILSRKLRIG HSNGKQLLKK LNAFGYTEAD VRQALEDE
