ID RNPA_YERPS Reviewed; 119 AA. AC Q663S9; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, 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}; GN OrderedLocusNames=YPTB3946; OS Yersinia pseudotuberculosis serotype I (strain IP32953). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=273123; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP32953; RX PubMed=15358858; DOI=10.1073/pnas.0404012101; RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M., RA Derbise A., Hauser L.J., Garcia E.; RT "Insights into the evolution of Yersinia pestis through whole-genome RT comparison with Yersinia pseudotuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004). 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; BX936398; CAH23184.1; -; Genomic_DNA. DR RefSeq; WP_002228153.1; NZ_CP009712.1. DR AlphaFoldDB; Q663S9; -. DR SMR; Q663S9; -. DR GeneID; 66843637; -. DR KEGG; ypo:BZ17_2630; -. DR KEGG; yps:YPTB3946; -. DR PATRIC; fig|273123.14.peg.2757; -. DR Proteomes; UP000001011; 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..119 FT /note="Ribonuclease P protein component" FT /id="PRO_0000198572" SQ SEQUENCE 119 AA; 13800 MW; 20C70729B34B5D24 CRC64; MVKLAFPREL RLLTPSHFTF VFQQPQRAGT PQITILGRLN ELGHPRIGLT VAKKHVKRAH ERNRIKRLTR ESFRLHQHAL PSMDFVVLVK KGVADLDNRA LTEALEKLWR RHCRQAPAS //