ID   RNM51_LIGS5             Reviewed;         191 AA.
AC   D8IJV0;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Ribonuclease M5 1 {ECO:0000255|HAMAP-Rule:MF_01469};
DE            EC=3.1.26.8 {ECO:0000255|HAMAP-Rule:MF_01469};
DE   AltName: Full=RNase M5 1 {ECO:0000255|HAMAP-Rule:MF_01469};
DE   AltName: Full=Ribosomal RNA terminal maturase M5 1 {ECO:0000255|HAMAP-Rule:MF_01469};
GN   Name=rnmV1 {ECO:0000255|HAMAP-Rule:MF_01469}; OrderedLocusNames=HN6_00222;
OS   Ligilactobacillus salivarius (strain CECT 5713) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=712961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5713;
RX   PubMed=20675488; DOI=10.1128/jb.00703-10;
RA   Jimenez E., Martin R., Maldonado A., Martin V., Gomez de Segura A.,
RA   Fernandez L., Rodriguez J.M.;
RT   "Complete genome sequence of Lactobacillus salivarius CECT 5713, a
RT   probiotic strain isolated from human milk and infant feces.";
RL   J. Bacteriol. 192:5266-5267(2010).
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; CP002034; ADJ78552.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8IJV0; -.
DR   SMR; D8IJV0; -.
DR   KEGG; lsi:HN6_00222; -.
DR   PATRIC; fig|712961.3.peg.1734; -.
DR   HOGENOM; CLU_109405_0_0_9; -.
DR   OMA; RLQMFQI; -.
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   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   Ribosome biogenesis; RNA-binding; rRNA processing; rRNA-binding.
FT   CHAIN           1..191
FT                   /note="Ribonuclease M5 1"
FT                   /id="PRO_0000416749"
FT   DOMAIN          10..93
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         16
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         62
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         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ   SEQUENCE   191 AA;  21513 MW;  F072F12419D89B14 CRC64;
     MNENDKMKIK EVIVVEGKDD TKRIQMAVNA DTLETRGSAI SDETLDQIED LYDKRGVIVF
     TDPDFSGEKI RKIITEAVPG VKHAFLTKHD AAPSHKGSLG VEHASPEAIR EALAHLYTEV
     PDGEPLISRE DLAVAGLTSG PQAKEYRRRL GEYLRIGYTN GKQLYKRLKL FQITPDELKK
     ALEYIKNEDN Y