ID A0A221MHX1_9BACI Unreviewed; 114 AA.
AC A0A221MHX1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Ribonuclease P protein component {ECO:0000256|HAMAP-Rule:MF_00227};
DE Short=RNase P protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE Short=RNaseP protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00227};
DE AltName: Full=Protein C5 {ECO:0000256|HAMAP-Rule:MF_00227};
GN Name=rnpA {ECO:0000256|HAMAP-Rule:MF_00227};
GN ORFNames=CFK40_01645 {ECO:0000313|EMBL:ASN07258.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN07258.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN07258.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN07258.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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:0000256|ARBA:ARBA00002663, ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00227};
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC protein subunit. {ECO:0000256|HAMAP-Rule:MF_00227}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; CP022437; ASN07258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221MHX1; -.
DR KEGG; vne:CFK40_01645; -.
DR OrthoDB; 9810867at2; -.
DR Proteomes; UP000204391; 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 {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00227};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00227};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00227};
KW Reference proteome {ECO:0000313|Proteomes:UP000204391};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00227}.
SQ SEQUENCE 114 AA; 13570 MW; 2A17F28073B4561A CRC64;
MKKAFRIKDN EEFQLLFKKG KSFANRQLVV YYMEKEGQAH FRIGISVGKK IGNAVTRNRI
KRHLRHAFQD LKEEIAKPSD IIIIARQPTK DMSYEQFKKS LIHLLSRERL IKKR
//