RNM5_LACPL
ID RNM5_LACPL Reviewed; 187 AA.
AC F9UU40;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=lp_0457;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC77960.1; -; Genomic_DNA.
DR RefSeq; WP_011101014.1; NC_004567.2.
DR RefSeq; YP_004888474.1; NC_004567.2.
DR AlphaFoldDB; F9UU40; -.
DR SMR; F9UU40; -.
DR STRING; 220668.lp_0457; -.
DR EnsemblBacteria; CCC77960; CCC77960; lp_0457.
DR KEGG; lpl:lp_0457; -.
DR PATRIC; fig|220668.9.peg.377; -.
DR eggNOG; COG1658; Bacteria.
DR HOGENOM; CLU_109405_0_0_9; -.
DR OMA; RLQMFQI; -.
DR PhylomeDB; F9UU40; -.
DR BioCyc; LPLA220668:G1GW0-381-MON; -.
DR Proteomes; UP000000432; 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-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
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 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..187
FT /note="Ribonuclease M5"
FT /id="PRO_0000416748"
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 187 AA; 20163 MW; 515E1550742030E4 CRC64;
MKKIKEVIVV EGKDDTKRLA LAVDADTLET NGSAISEATL AQIKTLQASR GVIVFTDPDF
SGERIRKTIS AAVPGVKHAF LPRKAGVPTK AGGSLGVEHA SPAAIQTALA HLYTEQIDEP
QQLISHHDLI AAGLLAGPTA RQRREQLGER LGIGYVNGKQ LPKRLQLFQI QPADFWAAVD
QLTTEEK
