ID   RSMG_MYCLE              Reviewed;         245 AA.
AC   Q50203;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00074};
DE   AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE            Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE   AltName: Full=Glucose-inhibited division protein B;
GN   Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; Synonyms=gidB;
GN   OrderedLocusNames=ML2708;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8969512; DOI=10.1099/13500872-142-11-3147;
RA   Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G.,
RA   Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.;
RT   "Gene arrangement and organization in an approximately 76 kb fragment
RT   encompassing the oriC region of the chromosome of Mycobacterium leprae.";
RL   Microbiology 142:3147-3161(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC       position 518 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC       methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC32240.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L39923; AAB53136.1; -; Genomic_DNA.
DR   EMBL; AL583926; CAC32240.1; ALT_INIT; Genomic_DNA.
DR   PIR; B87248; B87248.
DR   RefSeq; WP_010909047.1; NC_002677.1.
DR   AlphaFoldDB; Q50203; -.
DR   SMR; Q50203; -.
DR   STRING; 272631.ML2708; -.
DR   EnsemblBacteria; CAC32240; CAC32240; CAC32240.
DR   KEGG; mle:ML2708; -.
DR   Leproma; ML2708; -.
DR   eggNOG; COG0357; Bacteria.
DR   HOGENOM; CLU_065341_5_0_11; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR   InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR31760; PTHR31760; 1.
DR   Pfam; PF02527; GidB; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="Ribosomal RNA small subunit methyltransferase G"
FT                   /id="PRO_0000184281"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         140..141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   CONFLICT        227..245
FT                   /note="RCGQQMRHKPARVGDRKTQ -> DADSRCGTNQRVWGTGKHN (in Ref.
FT                   1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27044 MW;  5A7DED003227AAAA CRC64;
     MKHVGSYEEL ASFTSVKGNL GFDTVFEAVF MIFGPRLNIA QRYVDLLANT GIERGLLGPH
     EANRLWDRHL LNSAVVAELL DPGDRVVDIG SGAGLPGLPL AIARPDLQVV LLEPLLRRVT
     FLREVVAELG LDVEVVRGRA EELWVRDRIG ERDVAVSRAV AALDKLTKWS IPLLRPGGQI
     LAIKGEHVFD EIHQHRRVMA SLGAVDVMVV VCGANYLCRP VTVVLTRCGQ QMRHKPARVG
     DRKTQ