ID   RNPA_STAAU              Reviewed;         117 AA.
AC   P0A0H5; P58031; Q9LAH9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ISP3;
RA   Poppe S.M., Swaney S.M., Choi G.H., Hromockyj A., Shinabarger D.L.;
RT   "Cloning and characterization of Staphylococcus aureus ribonuclease P.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=10623511; DOI=10.1006/jmbi.1999.3341;
RA   Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D.,
RA   Hegg L.A., Eggleston D.S.;
RT   "The structure of ribonuclease P protein from Staphylococcus aureus reveals
RT   a unique binding site for single-stranded RNA.";
RL   J. Mol. Biol. 295:105-115(2000).
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00227}.
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DR   EMBL; AF135268; AAF61418.1; -; Genomic_DNA.
DR   RefSeq; WP_001789343.1; NZ_WYDB01000001.1.
DR   PDB; 1D6T; NMR; -; A=1-117.
DR   PDB; 6D1R; X-ray; 2.00 A; A=4-117.
DR   PDB; 6OV1; X-ray; 1.66 A; A/B=4-117.
DR   PDBsum; 1D6T; -.
DR   PDBsum; 6D1R; -.
DR   PDBsum; 6OV1; -.
DR   AlphaFoldDB; P0A0H5; -.
DR   SMR; P0A0H5; -.
DR   BindingDB; P0A0H5; -.
DR   ChEMBL; CHEMBL4295710; -.
DR   OMA; PEQKHFR; -.
DR   EvolutionaryTrace; P0A0H5; -.
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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
DR   InterPro; IPR020539; RNase_P_CS.
DR   PANTHER; PTHR33992; PTHR33992; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR00188; rnpA; 1.
DR   PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endonuclease; Hydrolase; Nuclease; RNA-binding;
KW   tRNA processing.
FT   CHAIN           1..117
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_0000198530"
FT   HELIX           5..7
FT                   /evidence="ECO:0007829|PDB:1D6T"
FT   HELIX           12..21
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   HELIX           56..73
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   HELIX           88..92
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   HELIX           95..108
FT                   /evidence="ECO:0007829|PDB:6OV1"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:1D6T"
SQ   SEQUENCE   117 AA;  13652 MW;  AD5172C3654E01F0 CRC64;
     MLLEKAYRIK KNADFQRIYK KGHSVANRQF VVYTCNNKEI DHFRLGISVS KKLGNAVLRN
     KIKRAIRENF KVHKSHILAK DIIVIARQPA KDMTTLQIQN SLEHVLKIAK VFNKKIK