ID   RNPA_HELPY              Reviewed;         161 AA.
AC   P55997;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   04-NOV-2026, entry version 125.
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=HP_1448;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD08489.1; -; Genomic_DNA.
DR   PIR; H64700; H64700.
DR   RefSeq; WP_001112484.1; NC_018939.1.
DR   SMR; P55997; -.
DR   DIP; DIP-3737N; -.
DR   IntAct; P55997; 5.
DR   STRING; 85962.HP_1448; -.
DR   PaxDb; 85962-HP_1448; -.
DR   EnsemblBacteria; AAD08489; AAD08489; HP_1448.
DR   KEGG; heo:C694_07500; -.
DR   KEGG; hpy:HP_1448; -.
DR   PATRIC; fig|85962.47.peg.1557; -.
DR   eggNOG; COG0594; Bacteria.
DR   InParanoid; P55997; -.
DR   OMA; ACSKVIH; -.
DR   OrthoDB; 9810867at2; -.
DR   PhylomeDB; P55997; -.
DR   FunFam; 3.30.230.10:FF:000143; Ribonuclease P protein component; 1.
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   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   NCBIfam; TIGR00188; rnpA; 1.
DR   PROSITE; PS00648; RIBONUCLEASE_P; 1.
DR   GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042780; P:tRNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000000429; Chromosome.
DR   AlphaFoldDB; P55997; -.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW   tRNA processing.
FT   CHAIN           1..161
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000198469"
SQ   SEQUENCE   161 AA;  18753 MW;  A2F561C92AEE9515 CRC64;
     MPDELRAEKS FPSKPYDSLK NKSEFDRVYQ KGFKKHNPFF SLFVLDLSQE PPKEKAGFKD
     PLFCRLKDKK TLYLLGLSVS KKVGNAVKRN LIKRRLRSLT LKHAALCQGL ALVFVPRSDC
     YHLDFWALEK HFLEMLTSIK NYMNKALKDL KKGITHTYAK Q
//