ID   RNPA_CHLPN              Reviewed;         139 AA.
AC   Q9Z6X2; Q9JQ16;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 129.
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=CPn_0934, CP_0927, CpB0967;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD19072.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF73717.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA99142.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98897.1; -; Genomic_DNA.
DR   PIR; D86607; D86607.
DR   PIR; H72016; H72016.
DR   RefSeq; NP_225129.1; NC_000922.1.
DR   RefSeq; WP_010883569.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z6X2; -.
DR   SMR; Q9Z6X2; -.
DR   STRING; 115711.CP_0927; -.
DR   EnsemblBacteria; AAD19072; AAD19072; CPn_0934.
DR   EnsemblBacteria; AAF73717; AAF73717; CP_0927.
DR   GeneID; 45050990; -.
DR   KEGG; cpa:CP_0927; -.
DR   KEGG; cpj:rnpA; -.
DR   KEGG; cpn:CPn_0934; -.
DR   KEGG; cpt:CpB0967; -.
DR   PATRIC; fig|115713.3.peg.1022; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_9_2_0; -.
DR   OrthoDB; 2014742at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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   PANTHER; PTHR33992; PTHR33992; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00188; rnpA; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT   CHAIN           1..139
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000198446"
FT   REGION          120..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   139 AA;  15927 MW;  FEA124BF77FEF23D CRC64;
     MHPLTLPKQS RVLKRKQFLY ITRSGFCCRG SQATFYVVPS RHPGTCRMGI TVSKKFGKAH
     ERNSFKRVVR EVFRHVRHQL PNCQIVVFPK GHKQRPVFSK LLQDFINQIP EGLHRLGKTK
     ATTGGECTPK SEKCVTAPR