ID RNPA_LISIN Reviewed; 119 AA.
AC Q926Q4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 29-MAY-2013, entry version 63.
DE RecName: Full=Ribonuclease P protein component;
DE Short=RNase P protein;
DE Short=RNaseP protein;
DE EC=3.1.26.5;
DE AltName: Full=Protein C5;
GN Name=rnpA; OrderedLocusNames=lin2987;
OS Listeria innocua serovar 6a (strain CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence
CC from pre-tRNA to produce the mature 5'-terminus. It can also
CC cleave other RNA substrates such as 4.5S RNA. The protein
CC component plays an auxiliary but essential role in vivo by binding
CC to the 5'-leader sequence and broadening the substrate specificity
CC of the ribozyme (By similarity).
CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'-
CC extranucleotides from tRNA precursor.
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or RnpB) and a
CC protein subunit (By similarity).
CC -!- SIMILARITY: Belongs to the RnpA family.
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DR EMBL; AL596174; CAC98212.1; -; Genomic_DNA.
DR PIR; AD1805; AD1805.
DR RefSeq; NP_472313.1; NC_003212.1.
DR ProteinModelPortal; Q926Q4; -.
DR SMR; Q926Q4; 1-112.
DR STRING; 272626.lin2987; -.
DR EnsemblBacteria; CAC98212; CAC98212; CAC98212.
DR GeneID; 1131876; -.
DR KEGG; lin:lin2987; -.
DR PATRIC; 20302920; VBILisInn102668_3064.
DR GenoList; LIN2987; -.
DR eggNOG; COG0594; -.
DR HOGENOM; HOG000266301; -.
DR KO; K03536; -.
DR OMA; KIGNAVM; -.
DR ProtClustDB; PRK00499; -.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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 Pfam; PF00825; Ribonuclease_P; 1.
DR ProDom; PD003629; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
DR PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE 3: Inferred from homology;
KW Complete proteome; Endonuclease; Hydrolase; Nuclease; RNA-binding;
KW tRNA processing.
FT CHAIN 1 119 Ribonuclease P protein component.
FT /FTId=PRO_0000198478.
SQ SEQUENCE 119 AA; 14132 MW; 179F13091B5827BD CRC64;
MKKKYRIKKN DDFQKVFRRG KSFANRQFVV YTLKQEEASH FRIGLSVSKK IGNAVCRNRI
KRYIRQSFHE LESQINPENE YIIIARKPAA NMDFHEVKKS LIHVLKVGRV LKQKPNNSK
//
