RLME_ECOLI
ID RLME_ECOLI Reviewed; 209 AA.
AC P0C0R7; P28692; Q2M933;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase E;
DE EC=2.1.1.166;
DE AltName: Full=23S rRNA Um2552 methyltransferase;
DE AltName: Full=Cell division protein FtsJ;
DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase;
GN Name=rlmE; Synonyms=ftsJ, mrsF, rrmJ; OrderedLocusNames=b3179, JW3146;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8444796; DOI=10.1128/jb.175.5.1344-1351.1993;
RA Tomoyasu T., Yuki T., Morimura S., Mori H., Yamanaka K., Niki H.,
RA Hiraga S., Ogura T.;
RT "The Escherichia coli FtsH protein is a prokaryotic member of a protein
RT family of putative ATPases involved in membrane functions, cell cycle
RT control, and gene expression.";
RL J. Bacteriol. 175:1344-1351(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Wang R., Kushner S.R.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=10748051; DOI=10.1074/jbc.m001854200;
RA Caldas T., Binet E., Bouloc P., Costa A., Desgres J., Richarme G.;
RT "The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23S ribosomal
RT RNA methyltransferase.";
RL J. Biol. Chem. 275:16414-16419(2000).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10814528; DOI=10.1006/bbrc.2000.2702;
RA Caldas T., Binet E., Bouloc P., Richarme G.;
RT "Translational defects of Escherichia coli mutants deficient in the
RT Um(2552) 23S ribosomal RNA methyltransferase RrmJ/FtsJ.";
RL Biochem. Biophys. Res. Commun. 271:714-718(2000).
RN [7]
RP DISRUPTION PHENOTYPE, AND RESCUE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11976298; DOI=10.1128/jb.184.10.2692-2698.2002;
RA Tan J., Jakob U., Bardwell J.C.A.;
RT "Overexpression of two different GTPases rescues a null mutation in a heat-
RT induced rRNA methyltransferase.";
RL J. Bacteriol. 184:2692-2698(2002).
RN [8]
RP ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-38;
RP ASP-83; ASP-124; LYS-164; GLU-199 AND TYR-201.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12181314; DOI=10.1074/jbc.m205423200;
RA Hager J., Staker B.L., Buegl H., Jakob U.;
RT "Active site in RrmJ, a heat shock-induced methyltransferase.";
RL J. Biol. Chem. 277:41978-41986(2002).
RN [9]
RP MUTAGENESIS OF ASP-20; TYR-22; ARG-32; ARG-34; ASP-136; LYS-189; ARG-194
RP AND SER-197.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15375145; DOI=10.1128/jb.186.19.6634-6642.2004;
RA Hager J., Staker B.L., Jakob U.;
RT "Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.";
RL J. Bacteriol. 186:6634-6642(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 30-209 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND DISRUPTION PHENOTYPE.
RX PubMed=10983982; DOI=10.1016/s1097-2765(00)00035-6;
RA Buegl H., Fauman E.B., Staker B.L., Zheng F., Kushner S.R., Saper M.A.,
RA Bardwell J.C.A., Jakob U.;
RT "RNA methylation under heat shock control.";
RL Mol. Cell 6:349-360(2000).
CC -!- FUNCTION: Specifically methylates the uridine in position 2552 of 23S
CC rRNA at the 2'-O position of the ribose in the fully assembled 50S
CC ribosomal subunit. {ECO:0000269|PubMed:10748051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-
CC methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202, Rhea:RHEA-COMP:10203,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.166;
CC Evidence={ECO:0000269|PubMed:10748051};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10748051};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for 23S rRNA within 50S ribosomal subunits
CC {ECO:0000269|PubMed:12181314};
CC KM=3.7 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12181314};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:12181314};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By heat shock.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a dramatically
CC altered ribosome profile, a severe growth disadvantage, and a
CC temperature-sensitive phenotype. These effects are overcome by
CC overexpressing either of 2 small GTPases, ObgE/CgtA or EngA.
CC {ECO:0000269|PubMed:10983982, ECO:0000269|PubMed:11976298}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmE family.
CC {ECO:0000305}.
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DR EMBL; M83138; AAA23812.1; -; Genomic_DNA.
DR EMBL; U01376; AAA97507.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57980.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76211.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77223.1; -; Genomic_DNA.
DR PIR; S35108; S35108.
DR RefSeq; NP_417646.1; NC_000913.3.
DR RefSeq; WP_000145975.1; NZ_STEB01000012.1.
DR PDB; 1EIZ; X-ray; 1.70 A; A=30-209.
DR PDB; 1EJ0; X-ray; 1.50 A; A=30-209.
DR PDBsum; 1EIZ; -.
DR PDBsum; 1EJ0; -.
DR AlphaFoldDB; P0C0R7; -.
DR SMR; P0C0R7; -.
DR BioGRID; 4262423; 299.
DR DIP; DIP-47902N; -.
DR IntAct; P0C0R7; 22.
DR STRING; 511145.b3179; -.
DR jPOST; P0C0R7; -.
DR PaxDb; P0C0R7; -.
DR PRIDE; P0C0R7; -.
DR EnsemblBacteria; AAC76211; AAC76211; b3179.
DR EnsemblBacteria; BAE77223; BAE77223; BAE77223.
DR GeneID; 67415987; -.
DR GeneID; 947689; -.
DR KEGG; ecj:JW3146; -.
DR KEGG; eco:b3179; -.
DR PATRIC; fig|1411691.4.peg.3553; -.
DR EchoBASE; EB1470; -.
DR eggNOG; COG0293; Bacteria.
DR HOGENOM; CLU_009422_4_0_6; -.
DR InParanoid; P0C0R7; -.
DR OMA; HRQTDHL; -.
DR PhylomeDB; P0C0R7; -.
DR BioCyc; EcoCyc:EG11507-MON; -.
DR BioCyc; MetaCyc:EG11507-MON; -.
DR SABIO-RK; P0C0R7; -.
DR EvolutionaryTrace; P0C0R7; -.
DR PRO; PR:P0C0R7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IMP:EcoCyc.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:EcoCyc.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR004512; rRNA_MeTrfase_gammaproteobac.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00438; rrmJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Stress response; Transferase.
FT CHAIN 1..209
FT /note="Ribosomal RNA large subunit methyltransferase E"
FT /id="PRO_0000155497"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12181314"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10983982"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10983982"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10983982"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10983982"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:10983982"
FT MUTAGEN 20
FT /note="D->A: 2-fold decrease in activity. Increase in Km
FT for 50S subunit."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 22
FT /note="Y->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 32
FT /note="R->A: 4-fold decrease in activity and increase in Km
FT for 50S subunit; when associated with A-34."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 34
FT /note="R->A: 4-fold decrease in activity and increase in Km
FT for 50S subunit; when associated with A-32."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 38
FT /note="K->A: Loss of activity. Almost no change in S-
FT adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:12181314"
FT MUTAGEN 83
FT /note="D->A: 5-fold decrease in activity. Increase in Km
FT for 50S subunit and for S-adenosyl-L-methionine. Loss of S-
FT adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:12181314"
FT MUTAGEN 124
FT /note="D->A: Loss of activity. Loss of S-adenosyl-L-
FT methionine binding."
FT /evidence="ECO:0000269|PubMed:12181314"
FT MUTAGEN 136
FT /note="D->N: 2-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 164
FT /note="K->A: Loss of activity. No change in S-adenosyl-L-
FT methionine binding."
FT /evidence="ECO:0000269|PubMed:12181314"
FT MUTAGEN 189
FT /note="K->A: 9-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 194
FT /note="R->A: No change in activity. Increase in Km for 50S
FT subunit."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 197
FT /note="S->A: No change in activity. Increase in Km for 50S
FT subunit."
FT /evidence="ECO:0000269|PubMed:15375145"
FT MUTAGEN 199
FT /note="E->A: 16-fold decrease in activity. No change in S-
FT adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:12181314"
FT MUTAGEN 201
FT /note="Y->A: 5-fold decrease in activity. Almost no change
FT in S-adenosyl-L-methionine binding."
FT /evidence="ECO:0000269|PubMed:12181314"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1EJ0"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1EJ0"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1EJ0"
FT HELIX 133..154
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 155..168
FT /evidence="ECO:0007829|PDB:1EJ0"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1EJ0"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:1EJ0"
SQ SEQUENCE 209 AA; 23335 MW; B83C3A7DFA8AC78F CRC64;
MTGKKRSASS SRWLQEHFSD KYVQQAQKKG LRSRAWFKLD EIQQSDKLFK PGMTVVDLGA
APGGWSQYVV TQIGGKGRII ACDLLPMDPI VGVDFLQGDF RDELVMKALL ERVGDSKVQV
VMSDMAPNMS GTPAVDIPRA MYLVELALEM CRDVLAPGGS FVVKVFQGEG FDEYLREIRS
LFTKVKVRKP DSSRARSREV YIVATGRKP
