RNPA_BACSU
ID RNPA_BACSU Reviewed; 116 AA.
AC P25814;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 150.
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=BSU41050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / CRK2000;
RX PubMed=1552862; DOI=10.1111/j.1365-2958.1992.tb01510.x;
RA Ogasawara N., Yoshikawa H.;
RT "Genes and their organization in the replication origin region of the
RT bacterial chromosome.";
RL Mol. Microbiol. 6:629-634(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-116.
RC STRAIN=168;
RX PubMed=1487728; DOI=10.1099/00221287-138-12-2609;
RA Errington J., Appleby L., Daniel R.A., Goodfellow H., Partridge S.R.,
RA Yudkin M.D.;
RT "Structure and function of the spoIIIJ gene of Bacillus subtilis: a
RT vegetatively expressed gene that is essential for sigma G activity at an
RT intermediate stage of sporulation.";
RL J. Gen. Microbiol. 138:2609-2618(1992).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9628904; DOI=10.1093/nar/26.13.3090;
RA Niranjanakumari S., Kurz J.C., Fierke C.A.;
RT "Expression, purification and characterization of the recombinant
RT ribonuclease P protein component from Bacillus subtilis.";
RL Nucleic Acids Res. 26:3090-3096(1998).
RN [6]
RP INTERACTION WITH CSHA, AND SUBUNIT.
RX PubMed=21764917; DOI=10.1128/jb.05485-11;
RA Roux C.M., DeMuth J.P., Dunman P.M.;
RT "Characterization of components of the Staphylococcus aureus mRNA
RT degradosome holoenzyme-like complex.";
RL J. Bacteriol. 193:5520-5526(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9563955; DOI=10.1126/science.280.5364.752;
RA Stams T., Niranjanakumari S., Fierke C.A., Christianson D.W.;
RT "Ribonuclease P protein structure: evolutionary origins in the
RT translational apparatus.";
RL Science 280:752-755(1998).
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 -!- 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. Might be a component of the prossible RNA degradosome
CC complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, and possibly
CC also rnpA. Interacts with RNA helicase CshA. {ECO:0000255|HAMAP-
CC Rule:MF_00227, ECO:0000269|PubMed:21764917}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA44400.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X62539; CAA44400.1; ALT_INIT; Genomic_DNA.
DR EMBL; D26185; BAA05235.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16142.1; -; Genomic_DNA.
DR EMBL; Z14225; CAA78594.1; -; Genomic_DNA.
DR PIR; I40436; JQ1214.
DR RefSeq; NP_391985.1; NC_000964.3.
DR RefSeq; WP_003242628.1; NZ_JNCM01000034.1.
DR PDB; 1A6F; X-ray; 2.60 A; A=2-116.
DR PDB; 4JG4; X-ray; 2.30 A; A=2-116.
DR PDBsum; 1A6F; -.
DR PDBsum; 4JG4; -.
DR AlphaFoldDB; P25814; -.
DR SMR; P25814; -.
DR IntAct; P25814; 2.
DR STRING; 224308.BSU41050; -.
DR PaxDb; P25814; -.
DR PRIDE; P25814; -.
DR EnsemblBacteria; CAB16142; CAB16142; BSU_41050.
DR GeneID; 937930; -.
DR KEGG; bsu:BSU41050; -.
DR PATRIC; fig|224308.179.peg.4447; -.
DR eggNOG; COG0594; Bacteria.
DR InParanoid; P25814; -.
DR OMA; PEQKHFR; -.
DR PhylomeDB; P25814; -.
DR BioCyc; BSUB:BSU41050-MON; -.
DR BRENDA; 3.1.26.5; 658.
DR SABIO-RK; P25814; -.
DR EvolutionaryTrace; P25814; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:CAFA.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IDA:CAFA.
DR GO; GO:0043168; F:anion binding; IDA:CAFA.
DR GO; GO:0031404; F:chloride ion binding; IDA:CAFA.
DR GO; GO:0042301; F:phosphate ion binding; IDA:CAFA.
DR GO; GO:0004526; F:ribonuclease P activity; IDA:CAFA.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:CAFA.
DR GO; GO:0043199; F:sulfate binding; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IDA:CAFA.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR DisProt; DP00387; -.
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 PANTHER; PTHR33992; PTHR33992; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
DR PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding; tRNA processing.
FT CHAIN 1..116
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198424"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4JG4"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4JG4"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:4JG4"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:4JG4"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4JG4"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:4JG4"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4JG4"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4JG4"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:4JG4"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:4JG4"
SQ SEQUENCE 116 AA; 13800 MW; E15CA6B7851716BE CRC64;
MKKRNRLKKN EDFQKVFKHG TSVANRQFVL YTLDQPENDE LRVGLSVSKK IGNAVMRNRI
KRLIRQAFLE EKERLKEKDY IIIARKPASQ LTYEETKKSL QHLFRKSSLY KKSSSK
