ID   RSMG_MYCS2              Reviewed;         235 AA.
AC   A0R7J5; I7GGS6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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};
GN   Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; Synonyms=gidB;
GN   OrderedLocusNames=MSMEG_6940, MSMEI_6748;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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=AFP43174.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK73841.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP43174.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_891133.1; NC_008596.1.
DR   AlphaFoldDB; A0R7J5; -.
DR   SMR; A0R7J5; -.
DR   STRING; 246196.MSMEI_6748; -.
DR   EnsemblBacteria; ABK73841; ABK73841; MSMEG_6940.
DR   EnsemblBacteria; AFP43174; AFP43174; MSMEI_6748.
DR   KEGG; msg:MSMEI_6748; -.
DR   KEGG; msm:MSMEG_6940; -.
DR   PATRIC; fig|246196.19.peg.6753; -.
DR   eggNOG; COG0357; Bacteria.
DR   OMA; WDRHVLN; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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..235
FT                   /note="Ribosomal RNA small subunit methyltransferase G"
FT                   /id="PRO_0000335376"
FT   REGION          211..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..235
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         124..125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   235 AA;  25732 MW;  3274B185CA0DADD5 CRC64;
     MKHGSVPATP EAASLVFGDR LEAAELYARI LAGAGVEWGL LGPREVDRVW ERHILNSAAL
     GELMEPGERV ADIGSGAGLP GIPLALARPD IHVTLIEPLL RRSEFLRETV TELGLDVTVV
     RGRAEDREVR DRVGEMDVVT SRAVASLDKL TRWSVPFLRD GGRMLPIKGE RAEVEIEEHR
     RVMESLGAVD ARVVRCGANY LSPPVTVVDA RRRAAKPGRN KSGRTARSRG RTGRR