ID   RSMG_RICAE              Reviewed;         192 AA.
AC   C3PM95;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=RAF_ORF0080;
OS   Rickettsia africae (strain ESF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=347255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESF-5;
RX   PubMed=19379498; DOI=10.1186/1471-2164-10-166;
RA   Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B.,
RA   Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.;
RT   "Analysis of the Rickettsia africae genome reveals that virulence
RT   acquisition in Rickettsia species may be explained by genome reduction.";
RL   BMC Genomics 10:166-166(2009).
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; CP001612; ACP53055.1; -; Genomic_DNA.
DR   RefSeq; WP_010976769.1; NC_012633.1.
DR   AlphaFoldDB; C3PM95; -.
DR   SMR; C3PM95; -.
DR   EnsemblBacteria; ACP53055; ACP53055; RAF_ORF0080.
DR   KEGG; raf:RAF_ORF0080; -.
DR   HOGENOM; CLU_065341_1_1_5; -.
DR   OMA; ICFPHLH; -.
DR   Proteomes; UP000002305; 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   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..192
FT                   /note="Ribosomal RNA small subunit methyltransferase G"
FT                   /id="PRO_1000202505"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         112..113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   192 AA;  22084 MW;  ED3285DE596CBCEC CRC64;
     MMEVPREIIE KLEIFQKLVK KWNKSINLVS DNTIHNFWQR HILDSLQLIQ YIDNKEIHLV
     DIGSGSGLPG IVLSIAGVAQ VSLIEADLRK CIFLEKASKI SNNNIQIINQ RIEKVEIDCS
     ILTCRAFSNL NTIFNCIKNI SVREKFLLLK GKNYLTEIVE AKERWLFGYL IHQSITCEEG
     KILEVSNLTK MI