ID   RNPA_STRU0              Reviewed;         119 AA.
AC   B9DVV7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
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=SUB1667;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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; AM946015; CAR43557.1; -; Genomic_DNA.
DR   RefSeq; WP_015911964.1; NC_012004.1.
DR   AlphaFoldDB; B9DVV7; -.
DR   SMR; B9DVV7; -.
DR   STRING; 218495.SUB1667; -.
DR   GeneID; 58022146; -.
DR   KEGG; sub:SUB1667; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_9_1_9; -.
DR   OrthoDB; 9810867at2; -.
DR   Proteomes; UP000000449; 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; Reference proteome; RNA-binding;
KW   tRNA processing.
FT   CHAIN           1..119
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_1000194679"
SQ   SEQUENCE   119 AA;  14008 MW;  4AAA3956EAE0B568 CRC64;
     MKKSYRVKRE KDFQAIFDGG KSTANRKFVI HFLEKEQDHY RVGISVGKRI GNAVTRNAVK
     RKIRHVIMEF SDHLKRDDFV VIARKGVENL DYQEVKQNLQ HVLKLANLLE EGFESEKKH
//