RNPA_MYCA9
ID RNPA_MYCA9 Reviewed; 127 AA.
AC B1MN96;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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}; OrderedLocusNames=MAB_4954c;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM65022.1; -; Genomic_DNA.
DR RefSeq; WP_012296830.1; NZ_MLCG01000007.1.
DR AlphaFoldDB; B1MN96; -.
DR SMR; B1MN96; -.
DR EnsemblBacteria; CAM65022; CAM65022; MAB_4954c.
DR GeneID; 66970383; -.
DR KEGG; mab:MAB_4954c; -.
DR OMA; THHVVIR; -.
DR Proteomes; UP000007137; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR PANTHER; PTHR33992; PTHR33992; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT CHAIN 1..127
FT /note="Ribonuclease P protein component"
FT /id="PRO_1000100373"
FT REGION 99..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 127 AA; 14173 MW; A8FB932DB05A572B CRC64;
MLPTRHRMTK SSEFRQTVKR GVRTTHADLV IHLRRGCPDS ACEQVEGPKV GLIVGKSVGG
AVVRHRVSRR LRHAAAELLP KLEPVDRMVI RALPSSSTAL SASLRQQLRD GIDRSARRQE
PAAERQR
