ID   RNPA_ALCBS              Reviewed;         121 AA.
AC   Q0VKU6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=ABO_2754;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL18202.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0VKU6; -.
DR   SMR; Q0VKU6; -.
DR   STRING; 393595.ABO_2754; -.
DR   EnsemblBacteria; CAL18202; CAL18202; ABO_2754.
DR   KEGG; abo:ABO_2754; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_11_0_6; -.
DR   OMA; LHQHELP; -.
DR   Proteomes; UP000008871; 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; Reference proteome; RNA-binding;
KW   tRNA processing.
FT   CHAIN           1..121
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_1000078187"
SQ   SEQUENCE   121 AA;  14108 MW;  76B34DEAAE0CA3F7 CRC64;
     MPISQAFTRQ HRLLTGPQYQ TVFDQPEWKV GLGGYLLLVT RNSQPHPRLG LVIGRKRVKR
     AVDRARIKRR VREQFRCRQQ ELAGLDIILL VRGRIENPNP NQVTLDITRL FDKLLAKCRQ
     A