RNPA_ECOLI
ID RNPA_ECOLI Reviewed; 119 AA.
AC P0A7Y8; P06277; Q2M816;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=b3704, JW3681;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2415431; DOI=10.1016/0378-1119(85)90206-9;
RA Hansen F.G., Hansen E.B., Atlung T.;
RT "Physical mapping and nucleotide sequence of the rnpA gene that encodes the
RT protein component of ribonuclease P in Escherichia coli.";
RL Gene 38:85-93(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RX PubMed=6329723; DOI=10.1002/j.1460-2075.1982.tb01294.x;
RA Hansen F.G., Hansen E.B., Atlung T.;
RT "The nucleotide sequence of the dnaA gene promoter and of the adjacent rpmH
RT gene, coding for the ribosomal protein L34, of Escherichia coli.";
RL EMBO J. 1:1043-1048(1982).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND RNA-BINDING.
RX PubMed=22298511; DOI=10.1093/nar/gks013;
RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P.,
RA Gopalan V.;
RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional
RT dependence of archaeal and eukaryal RNase P on multiple protein
RT cofactors.";
RL Nucleic Acids Res. 40:4666-4680(2012).
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, ECO:0000269|PubMed:22298511}.
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, ECO:0000269|PubMed:22298511};
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227,
CC ECO:0000269|PubMed:22298511}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; M11056; AAA24567.1; -; Genomic_DNA.
DR EMBL; X01861; CAA25983.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62055.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76727.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77590.1; -; Genomic_DNA.
DR PIR; A00794; NRECP.
DR RefSeq; NP_418159.1; NC_000913.3.
DR RefSeq; WP_000239730.1; NZ_STEB01000015.1.
DR PDB; 2LJP; NMR; -; A=1-119.
DR PDBsum; 2LJP; -.
DR AlphaFoldDB; P0A7Y8; -.
DR SMR; P0A7Y8; -.
DR BioGRID; 4261766; 36.
DR BioGRID; 852517; 2.
DR DIP; DIP-36039N; -.
DR IntAct; P0A7Y8; 60.
DR STRING; 511145.b3704; -.
DR jPOST; P0A7Y8; -.
DR PaxDb; P0A7Y8; -.
DR PRIDE; P0A7Y8; -.
DR EnsemblBacteria; AAC76727; AAC76727; b3704.
DR EnsemblBacteria; BAE77590; BAE77590; BAE77590.
DR GeneID; 67417694; -.
DR GeneID; 948215; -.
DR KEGG; ecj:JW3681; -.
DR KEGG; eco:b3704; -.
DR PATRIC; fig|511145.12.peg.3828; -.
DR EchoBASE; EB0855; -.
DR eggNOG; COG0594; Bacteria.
DR HOGENOM; CLU_117179_11_0_6; -.
DR InParanoid; P0A7Y8; -.
DR OMA; LHQHELP; -.
DR PhylomeDB; P0A7Y8; -.
DR BioCyc; EcoCyc:EG10862-MON; -.
DR BioCyc; MetaCyc:EG10862-MON; -.
DR PRO; PR:P0A7Y8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:EcoCyc.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IDA:EcoliWiki.
DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:EcoliWiki.
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..119
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198458"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:2LJP"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:2LJP"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2LJP"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2LJP"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:2LJP"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2LJP"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2LJP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2LJP"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2LJP"
FT HELIX 98..117
FT /evidence="ECO:0007829|PDB:2LJP"
SQ SEQUENCE 119 AA; 13789 MW; 449D9EDACA1C6240 CRC64;
MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH
ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS
