ID   RNPA_CLOAB              Reviewed;         119 AA.
AC   Q97CV8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   28-JAN-2026, entry version 109.
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};
GN   OrderedLocusNames=CA_C3738;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM
OS   19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC
RC   13948 / NRRL B-527 / VKM B-1787 / 2291 / W;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81658.1; -; Genomic_DNA.
DR   PIR; G97358; G97358.
DR   RefSeq; WP_010966998.1; NC_003030.1.
DR   AlphaFoldDB; Q97CV8; -.
DR   SMR; Q97CV8; -.
DR   STRING; 272562.CA_C3738; -.
DR   GeneID; 45000234; -.
DR   KEGG; cac:CA_C3738; -.
DR   PATRIC; fig|272562.8.peg.3928; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_9_3_9; -.
DR   OrthoDB; 9810867at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:TreeGrafter.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:TreeGrafter.
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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
DR   NCBIfam; TIGR00188; rnpA; 1.
DR   PANTHER; PTHR33992; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR   PANTHER; PTHR33992:SF1; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW   tRNA processing.
FT   CHAIN           1..119
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000198450"
SQ   SEQUENCE   119 AA;  13889 MW;  3B474CEB3E54605C CRC64;
     MKENRIRKNA EFRRVYRKGK SFSNRLLVLY VYKNYILKDI NRIGISVSKK VGKSVVRSRV
     KRLIGESYRL NSSNLKKGHD FVIIARTACN GKRYSDIEDS IKNLFNKAGL VIYDEKNIT
//