ID   RNPA_STRM5              Reviewed;         152 AA.
AC   B4SPG1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   10-JUN-2026, 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};
GN   OrderedLocusNames=Smal_4044;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(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; CP001111; ACF53743.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4SPG1; -.
DR   SMR; B4SPG1; -.
DR   STRING; 391008.Smal_4044; -.
DR   PaxDb; 391008-Smal_4044; -.
DR   KEGG; smt:Smal_4044; -.
DR   eggNOG; COG0594; Bacteria.
DR   HOGENOM; CLU_117179_3_0_6; -.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:TreeGrafter.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:TreeGrafter.
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; Hydrolase; Nuclease; RNA-binding; tRNA processing.
FT   CHAIN           1..152
FT                   /note="Ribonuclease P protein component"
FT                   /id="PRO_1000100396"
FT   REGION          119..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   152 AA;  16879 MW;  1A222AF6274CC1C0 CRC64;
     MNTADPRKRF PRSARVRTRA EYSTVFNGAR RVSDPLMTLH WLPADRPARL GLAVSRKVDP
     HAVGRNRIKR VLRDALRQTR TDMQPGDFVV VARSAARNAS NDDIRQAFLR LLRRLRALPT
     PGVDGTMPPP DGIATPSLTE PAPRSGTAEP AR
//