ID   RNPA_CHLTB              Reviewed;         120 AA.
AC   B0BAN9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=CTLon_0153;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM884177; CAP06551.1; -; Genomic_DNA.
DR   RefSeq; WP_009873403.1; NC_010280.2.
DR   AlphaFoldDB; B0BAN9; -.
DR   SMR; B0BAN9; -.
DR   KEGG; ctl:CTLon_0153; -.
DR   HOGENOM; CLU_117179_9_2_0; -.
DR   Proteomes; UP001154401; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
DR   InterPro; IPR020539; RNase_P_CS.
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.
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_1000100349"
SQ   SEQUENCE   120 AA;  13761 MW;  77F43607B89E8ACC CRC64;
     MSRLTLPKNA RLLKRKQFVY VQRNGRCCRA DQVTLRVVPS RHSNTSKVGI TVSKKFGKAH
     QRNRFKRIVR EAFRHVRPNL PGCQVVISPR GNSQPDFLKL SEELLQRIPE ALPLASSSRC
//