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RLME_CERS4
ID   RLME_CERS4              Reviewed;         244 AA.
AC   Q3J2Q5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000255|HAMAP-Rule:MF_01547};
DE            EC=2.1.1.166 {ECO:0000255|HAMAP-Rule:MF_01547};
DE   AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547};
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547};
GN   Name=rlmE {ECO:0000255|HAMAP-Rule:MF_01547};
GN   Synonyms=ftsJ {ECO:0000255|HAMAP-Rule:MF_01547},
GN   rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; OrderedLocusNames=RHOS4_13610;
GN   ORFNames=RSP_2772;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01547}.
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:0000255|HAMAP-Rule:MF_01547};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01547}.
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DR   EMBL; CP000143; ABA78929.1; -; Genomic_DNA.
DR   RefSeq; WP_011337734.1; NZ_CP030271.1.
DR   RefSeq; YP_352830.1; NC_007493.2.
DR   AlphaFoldDB; Q3J2Q5; -.
DR   SMR; Q3J2Q5; -.
DR   STRING; 272943.RSP_2772; -.
DR   EnsemblBacteria; ABA78929; ABA78929; RSP_2772.
DR   KEGG; rsp:RSP_2772; -.
DR   PATRIC; fig|272943.9.peg.1696; -.
DR   eggNOG; COG0293; Bacteria.
DR   OMA; HRQTDHL; -.
DR   PhylomeDB; Q3J2Q5; -.
DR   Proteomes; UP000002703; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
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; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..244
FT                   /note="Ribosomal RNA large subunit methyltransferase E"
FT                   /id="PRO_0000282784"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
SQ   SEQUENCE   244 AA;  26284 MW;  F968AAD9690A90B3 CRC64;
     MTTKNTSGRG QRELRVRVKT AKGRKLSSTL WLERQLNDPY VIRAKKEGYR GRAAYKILEL
     DDKFGFLKPG GRVVDLGCAP GGWCQVAVER VNALGQKKNK PEGTVLGVDL QEVEPISGAE
     IHQLDFLSDD ADEKVKGWLG GRADVVMSDM AAAASGHKGT DHLRIIALCE AAAAFAFDVL
     EEGGTFVAKV LAGGAENELQ ALLKKNFTKV ANVKPPASRA DSSEKFVVAM GFRGRASEPE
     EGEA
 
 
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