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RNM5_BACCR
ID   RNM5_BACCR              Reviewed;         189 AA.
AC   Q81JA6;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=BC_0045;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP07143.1; -; Genomic_DNA.
DR   RefSeq; NP_829942.1; NC_004722.1.
DR   AlphaFoldDB; Q81JA6; -.
DR   SMR; Q81JA6; -.
DR   STRING; 226900.BC_0045; -.
DR   EnsemblBacteria; AAP07143; AAP07143; BC_0045.
DR   KEGG; bce:BC0045; -.
DR   PATRIC; fig|226900.8.peg.62; -.
DR   HOGENOM; CLU_109405_0_0_9; -.
DR   OMA; RLQMFQI; -.
DR   Proteomes; UP000001417; 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; PF13662; Toprim_4; 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..189
FT                   /note="Ribonuclease M5"
FT                   /id="PRO_0000416742"
FT   DOMAIN          8..91
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT   BINDING         14
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         60
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         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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"
SQ   SEQUENCE   189 AA;  21233 MW;  84470DB2FAF2B8B9 CRC64;
     MEASMKIKEI IVVEGKDDTV AIKRAVDADT IETNGSAIGD HVIEQVKLAQ QKRGVIIFTD
     PDYPGERIRK IISDKVPGCK HAFLPKEEAL AKRKKGVGIE HASNESIRRA LENIHEEMEA
     YTGEISWSDL VDAGLVGGEM AKSRRERMGK LLKIGYTNAK QLHKRLQMFQ VSKESFAEAY
     KQVIQEEKK
 
 
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