ID   RNPA_COXBU              Reviewed;         121 AA.
AC   P45648;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=CBU_1918;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Nine Mile phase I / Bratislava;
RX   PubMed=8071197; DOI=10.1128/jb.176.17.5233-5243.1994;
RA   Suhan M., Chen S.Y., Thompson H.A., Hoover T.A., Hill A., Williams J.C.;
RT   "Cloning and characterization of an autonomous replication sequence from
RT   Coxiella burnetii.";
RL   J. Bacteriol. 176:5233-5243(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO91409.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U10529; AAA56917.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO91409.2; ALT_INIT; Genomic_DNA.
DR   PIR; I40652; I40652.
DR   RefSeq; NP_820895.2; NC_002971.3.
DR   AlphaFoldDB; P45648; -.
DR   SMR; P45648; -.
DR   STRING; 227377.CBU_1918; -.
DR   EnsemblBacteria; AAO91409; AAO91409; CBU_1918.
DR   GeneID; 1209831; -.
DR   KEGG; cbu:CBU_1918; -.
DR   PATRIC; fig|227377.7.peg.1902; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_11_0_6; -.
DR   OMA; LHQHELP; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
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; Reference proteome; RNA-binding;
KW   tRNA processing.
FT   CHAIN           1..121
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000198455"
SQ   SEQUENCE   121 AA;  14398 MW;  E9402C53D6206EFE CRC64;
     MEKGFSVGWR IRTTAEFRRI YAARQRIIGR YYLLYYRENE IKHSRLGVVA SKRNVRKAVW
     RNRVRRVVKE AFRIRKKDLP AFDIVVVAKA SSVEADNKEL YECINKLFTQ LEKQSKRSSS
     V