RLMB_ECOLI
ID RLMB_ECOLI Reviewed; 243 AA.
AC P63177; P39290; Q2M6C5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB;
DE EC=2.1.1.185;
DE AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase;
DE AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase;
GN Name=rlmB; Synonyms=yjfH; OrderedLocusNames=b4180, JW4138;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11698387; DOI=10.1128/jb.183.23.6957-6960.2001;
RA Loevgren J.M., Wikstroem P.M.;
RT "The rlmB gene is essential for formation of Gm2251 in 23S rRNA but not for
RT ribosome maturation in Escherichia coli.";
RL J. Bacteriol. 183:6957-6960(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=12377117; DOI=10.1016/s0969-2126(02)00852-3;
RA Michel G., Sauve V., Larocque R., Li Y., Matte A., Cygler M.;
RT "The structure of the RlmB 23S rRNA methyltransferase reveals a new
RT methyltransferase fold with a unique knot.";
RL Structure 10:1303-1315(2002).
CC -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S
CC rRNA. {ECO:0000269|PubMed:11698387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24140, Rhea:RHEA-COMP:10239, Rhea:RHEA-COMP:10241,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.185;
CC Evidence={ECO:0000269|PubMed:11698387};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12377117}.
CC -!- INTERACTION:
CC P63177; P31806: nnr; NbExp=3; IntAct=EBI-562712, EBI-554188;
CC P63177; P0AF67: tsaE; NbExp=3; IntAct=EBI-562712, EBI-561268;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. RlmB subfamily.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97076.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77137.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78181.1; -; Genomic_DNA.
DR PIR; S56405; S56405.
DR RefSeq; NP_418601.1; NC_000913.3.
DR RefSeq; WP_001293282.1; NZ_STEB01000013.1.
DR PDB; 1GZ0; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-243.
DR PDBsum; 1GZ0; -.
DR AlphaFoldDB; P63177; -.
DR SMR; P63177; -.
DR BioGRID; 4261811; 37.
DR BioGRID; 852986; 2.
DR DIP; DIP-47866N; -.
DR IntAct; P63177; 19.
DR STRING; 511145.b4180; -.
DR jPOST; P63177; -.
DR PaxDb; P63177; -.
DR PRIDE; P63177; -.
DR EnsemblBacteria; AAC77137; AAC77137; b4180.
DR EnsemblBacteria; BAE78181; BAE78181; BAE78181.
DR GeneID; 67414798; -.
DR GeneID; 948694; -.
DR KEGG; ecj:JW4138; -.
DR KEGG; eco:b4180; -.
DR PATRIC; fig|1411691.4.peg.2521; -.
DR EchoBASE; EB2376; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_1_6; -.
DR InParanoid; P63177; -.
DR OMA; QVPPYEY; -.
DR PhylomeDB; P63177; -.
DR BioCyc; EcoCyc:G7845-MON; -.
DR BioCyc; MetaCyc:G7845-MON; -.
DR BRENDA; 2.1.1.185; 2026.
DR EvolutionaryTrace; P63177; -.
DR PRO; PR:P63177; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IMP:EcoCyc.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IMP:EcoCyc.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_01887; 23SrRNA_methyltr_B; 1.
DR InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR46429; PTHR46429; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR Pfam; PF08032; SpoU_sub_bind; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..243
FT /note="23S rRNA (guanosine-2'-O-)-methyltransferase RlmB"
FT /id="PRO_0000159785"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:1GZ0"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1GZ0"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:1GZ0"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1GZ0"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1GZ0"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:1GZ0"
SQ SEQUENCE 243 AA; 26557 MW; 6D6C4170580341D6 CRC64;
MSEMIYGIHA VQALLERAPE RFQEVFILKG REDKRLLPLI HALESQGVVI QLANRQYLDE
KSDGAVHQGI IARVKPGRQY QENDLPDLIA SLDQPFLLIL DGVTDPHNLG ACLRSADAAG
VHAVIVPKDR SAQLNATAKK VACGAAESVP LIRVTNLART MRMLQEENIW IVGTAGEADH
TLYQSKMTGR LALVMGAEGE GMRRLTREHC DELISIPMAG SVSSLNVSVA TGICLFEAVR
QRS
