ID   RNPA_THET8              Reviewed;         163 AA.
AC   Q7X5K6; Q5SL48;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=TTHA0445;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-61; 89-96; 125-154
RP   AND 158-163, CHARACTERIZATION, AND MUTAGENESIS.
RX   PubMed=12719542; DOI=10.1073/pnas.0931462100;
RA   Feltens R., Gossringer M., Willkomm D.K., Urlaub H., Hartmann R.K.;
RT   "An unusual mechanism of bacterial gene expression revealed for the RNase P
RT   protein of Thermus strains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5724-5729(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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   -!- 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.
CC   -!- MISCELLANEOUS: The open reading frame (ORF) for this protein entirely
CC       encompasses the ORF for the 50S ribosomal protein L34 (rpmH). The two
CC       start codons are separated by four nucleotides.
CC   -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00227}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD70268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY256342; AAO88977.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD70268.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_143711.1; NC_006461.1.
DR   AlphaFoldDB; Q7X5K6; -.
DR   SMR; Q7X5K6; -.
DR   STRING; 300852.55771827; -.
DR   EnsemblBacteria; BAD70268; BAD70268; BAD70268.
DR   KEGG; ttj:TTHA0445; -.
DR   PATRIC; fig|300852.9.peg.444; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_4_2_0; -.
DR   OMA; THENARW; -.
DR   Proteomes; UP000000532; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW   Reference proteome; RNA-binding; tRNA processing.
FT   CHAIN           1..163
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000198559"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         1..50
FT                   /note="Missing: No effect on activity of the reconstituted
FT                   enzyme."
FT                   /evidence="ECO:0000269|PubMed:12719542"
SQ   SEQUENCE   163 AA;  17851 MW;  7B30582D2C2D3421 CRC64;
     MDEKDVATQP QETGQNPRLS GQDEDPGRPE GAEAPPSEGA LAPHARRSEA VGPKPPAPGG
     KLLSLKGDRA FQRLRKGRAG RGRYVSVKWL PAAELRVGIV VSKKVGKAVV RNKVKRRLRE
     ILRRLHLPQA HLLVVASPEA READFAELFR DVVRALRKSG LVQ