RNM5_BORBU
ID RNM5_BORBU Reviewed; 181 AA.
AC O51571;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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}; OrderedLocusNames=BB_0626;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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}.
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DR EMBL; AE000783; AAC66987.1; -; Genomic_DNA.
DR PIR; A70178; A70178.
DR RefSeq; NP_212760.1; NC_001318.1.
DR RefSeq; WP_002657333.1; NC_001318.1.
DR AlphaFoldDB; O51571; -.
DR SMR; O51571; -.
DR STRING; 224326.BB_0626; -.
DR EnsemblBacteria; AAC66987; AAC66987; BB_0626.
DR GeneID; 56568701; -.
DR KEGG; bbu:BB_0626; -.
DR PATRIC; fig|224326.49.peg.1016; -.
DR HOGENOM; CLU_109405_0_0_12; -.
DR OMA; RLQMFQI; -.
DR Proteomes; UP000001807; 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; IEA:UniProtKB-EC.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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..181
FT /note="Ribonuclease M5"
FT /id="PRO_0000416743"
FT DOMAIN 5..88
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 11
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 57
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 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ SEQUENCE 181 AA; 20699 MW; 02BE2F310A93CBB0 CRC64;
MEKIKEIIVV EGKDDLKRIK ESFDCTVIET KGFALKIETI KLLKKALKYK GIIILTDSDK
SGNIIRQKIV KYLGENNKIK HAYLNTKDTE VESVNKTEII KILKGVGTLS KDNQKDLLKL
SDLLELGIIG ENSKENRQKI QKHFCLGDGN SKKLLERLNY FKIKKTDLKN QLALTNSPRR
T
