ID   RNPA_BORRA              Reviewed;         114 AA.
AC   B5RRP4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
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=BRE_442;
OS   Borrelia recurrentis (strain A1).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borrelia.
OX   NCBI_TaxID=412418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(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}.
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DR   EMBL; CP000993; ACH94678.1; -; Genomic_DNA.
DR   RefSeq; WP_012538195.1; NC_011244.1.
DR   AlphaFoldDB; B5RRP4; -.
DR   SMR; B5RRP4; -.
DR   KEGG; bre:BRE_442; -.
DR   HOGENOM; CLU_2116283_0_0_12; -.
DR   Proteomes; UP000000612; 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   NCBIfam; TIGR00188; rnpA; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT   CHAIN           1..114
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_1000194615"
SQ   SEQUENCE   114 AA;  13727 MW;  EEA21A790F45C1B7 CRC64;
     MKKRNINIKS RLEIQELFKK GQFVKIEGIN IFYRFTSLAI SRILITFPRV FKGAVKRNRV
     RRVFKECFRE YFTLLKDGCA DFIFVVYPQK ANINYHEVKT ILKNMIVYVI KRKV
//