ID   RNPA_RICBR              Reviewed;         120 AA.
AC   Q1RI66;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227};
DE            Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE            Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227};
DE   AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227};
GN   Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; OrderedLocusNames=RBE_0867;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from
CC       pre-tRNA to produce the mature 5'-terminus. It can also cleave other
CC       RNA substrates such as 4.5S RNA. The protein component plays an
CC       auxiliary but essential role in vivo by binding to the 5'-leader
CC       sequence and broadening the substrate specificity of the ribozyme.
CC       {ECO:0000255|HAMAP-Rule:MF_00227}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00227};
CC   -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC       protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}.
CC   -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00227}.
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DR   EMBL; CP000087; ABE04948.1; -; Genomic_DNA.
DR   RefSeq; WP_011477533.1; NC_007940.1.
DR   AlphaFoldDB; Q1RI66; -.
DR   SMR; Q1RI66; -.
DR   STRING; 336407.RBE_0867; -.
DR   EnsemblBacteria; ABE04948; ABE04948; RBE_0867.
DR   KEGG; rbe:RBE_0867; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_2047938_0_0_5; -.
DR   OMA; MRIIVND; -.
DR   OrthoDB; 2014742at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_00227; RNase_P; 1.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
DR   InterPro; IPR020539; RNase_P_CS.
DR   PANTHER; PTHR33992; PTHR33992; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00188; rnpA; 1.
DR   PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT   CHAIN           1..120
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000274855"
SQ   SEQUENCE   120 AA;  14145 MW;  DA04DA4237AF677C CRC64;
     MFITSLKNQK EFELINKLGK KFHEKYFILV IAKNIPKIFL ESKYNIFLGI KVSKKLNKKA
     VVRNKIKRRI KHLIRLICNN SNLKKLAMII IPRKGFDTAD FSVLNHELSK AILDFYNPKK