ID   RSMG_CAMJR              Reviewed;         188 AA.
AC   Q5HUG5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE            EC=2.1.1.170 {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};
GN   Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; OrderedLocusNames=CJE1077;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
CC   -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC       position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC         methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74480; EC=2.1.1.170; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CP000025; AAW35405.1; -; Genomic_DNA.
DR   RefSeq; WP_011049829.1; NC_003912.7.
DR   AlphaFoldDB; Q5HUG5; -.
DR   SMR; Q5HUG5; -.
DR   KEGG; cjr:CJE1077; -.
DR   HOGENOM; CLU_065341_2_1_7; -.
DR   OMA; IECELSN; -.
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   PIRSF; PIRSF003078; GidB; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..188
FT                   /note="Ribosomal RNA small subunit methyltransferase G"
FT                   /id="PRO_0000184232"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         119..120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   188 AA;  22323 MW;  4ACB610AD5D151B2 CRC64;
     MIFKDYDFLQ NYDLKNFEEK VKIYKELLSK FNRIHNLTHL KNIDENIFDS IKILDFYDFS
     KAKNIADIGS GAGFPAVFLA FLLQGNFHLF EPNPKKAAFL RTLKIECELS NLHIYKEKVQ
     EYQNIFKADI ITSRALMDVK PLLEICKNLK DENTVFILWK GSEIYQELEN IKDYEIFENN
     LRKYCILK