ID   RLMG_ECO5E              Reviewed;         378 AA.
AC   B5YRC4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_01859};
DE            EC=2.1.1.174 {ECO:0000255|HAMAP-Rule:MF_01859};
DE   AltName: Full=23S rRNA m2G1835 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01859};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmG {ECO:0000255|HAMAP-Rule:MF_01859};
GN   Name=rlmG {ECO:0000255|HAMAP-Rule:MF_01859};
GN   OrderedLocusNames=ECH74115_4398;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
CC   -!- FUNCTION: Specifically methylates the guanine in position 1835
CC       (m2G1835) of 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01859}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42744, Rhea:RHEA-COMP:10217, Rhea:RHEA-COMP:10218,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.174;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01859};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01859}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.
CC       {ECO:0000255|HAMAP-Rule:MF_01859}.
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DR   EMBL; CP001164; ACI38394.1; -; Genomic_DNA.
DR   RefSeq; WP_000018678.1; NC_011353.1.
DR   AlphaFoldDB; B5YRC4; -.
DR   SMR; B5YRC4; -.
DR   KEGG; ecf:ECH74115_4398; -.
DR   HOGENOM; CLU_040288_4_0_6; -.
DR   OMA; DFLAWRM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052916; F:23S rRNA (guanine(1835)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR017237; rRNA_m2G-MeTrfase_RsmD.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47816:SF5; PTHR47816:SF5; 1.
DR   Pfam; PF05175; MTS; 1.
DR   PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..378
FT                   /note="Ribosomal RNA large subunit methyltransferase G"
FT                   /id="PRO_0000366461"
SQ   SEQUENCE   378 AA;  42324 MW;  0EA9DDBC4CA8C5EF CRC64;
     MSHLDNGFRS LTLQRFPATD DVNPLQAWEA ADEYLLQQLD DTEIRGPVLI LNDAFGALSC
     ALAEHKPYSI GDSYISELAT RENLRLNGID ESSVKFLDST ADYPQQPGVV LIKVPKTLAL
     LEQQLRALRK VVTPQTRIIA GAKARDIHTS TLELFEKVLG PTTTTLAWKK ARLINCTFNE
     PPLADAPQTV SWKLEGTDWT IHNHANVFSR TGLDIGARFF MQHLPENLEG EIVDLGCGNG
     VIGLTLLDKN PQAKVVFVDE SPMAVASSRL NVETNMPEAL DRCEFMINNA LSGVEPFRFN
     AVLCNPPFHQ QHALTDNVAW EMFHHARRCL KINGELYIVA NRHLDYFHKL KKIFGNCTTI
     ATNNKFVVLK AVKLGRRR