ID RNPA_BIFLS Reviewed; 119 AA. AC B7GPF7; E8MPR7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-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=Blon_2498, BLIJ_2569; OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM OS 1222 / NCTC 11817 / S12). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=391904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12; RX PubMed=19033196; DOI=10.1073/pnas.0809584105; RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., RA Richardson P.M., Mills D.A.; RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals RT adaptations for milk utilization within the infant microbiome."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12; RX PubMed=21270894; DOI=10.1038/nature09646; RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., RA Morita H., Hattori M., Ohno H.; RT "Bifidobacteria can protect from enteropathogenic infection through RT production of acetate."; RL Nature 469:543-547(2011). 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; CP001095; ACJ53552.1; -; Genomic_DNA. DR EMBL; AP010889; BAJ70146.1; -; Genomic_DNA. DR RefSeq; WP_012578708.1; NZ_JDTT01000013.1. DR AlphaFoldDB; B7GPF7; -. DR SMR; B7GPF7; -. DR KEGG; bln:Blon_2498; -. DR KEGG; blon:BLIJ_2569; -. DR PATRIC; fig|391904.8.peg.2573; -. DR HOGENOM; CLU_117179_4_0_11; -. DR Proteomes; UP000001360; 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 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. PE 3: Inferred from homology; KW Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing. FT CHAIN 1..119 FT /note="Ribonuclease P protein component" FT /id="PRO_1000194610" SQ SEQUENCE 119 AA; 13346 MW; C9C2046F5157152F CRC64; MERLQSHRDF VTVLKRRRKA GGKDIVVHYL VPDDHHDDDD RTVHRRLGLA VSKSVGHAVT RNTVKRRFRV LARAHEDLLP AHCDIVLRAK PSAATASFVS LDQQIAKAFA TVAHKVAEA //