ID   RSMG_PARL1              Reviewed;         226 AA.
AC   A7HSL2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Plav_1275;
OS   Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Parvibaculaceae; Parvibaculum.
OX   NCBI_TaxID=402881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX   PubMed=22675581; DOI=10.4056/sigs.2215005;
RA   Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA   Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA   Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT   "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT   1(T)).";
RL   Stand. Genomic Sci. 5:298-310(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000774; ABS62895.1; -; Genomic_DNA.
DR   RefSeq; WP_012110167.1; NC_009719.1.
DR   AlphaFoldDB; A7HSL2; -.
DR   SMR; A7HSL2; -.
DR   STRING; 402881.Plav_1275; -.
DR   EnsemblBacteria; ABS62895; ABS62895; Plav_1275.
DR   KEGG; pla:Plav_1275; -.
DR   eggNOG; COG0357; Bacteria.
DR   HOGENOM; CLU_065341_1_1_5; -.
DR   OMA; ICFPHLH; -.
DR   OrthoDB; 1590629at2; -.
DR   Proteomes; UP000006377; 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..226
FT                   /note="Ribosomal RNA small subunit methyltransferase G"
FT                   /id="PRO_0000335390"
FT   REGION          199..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         136..137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT   BINDING         152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   226 AA;  24833 MW;  6E413A816C6AD0CB CRC64;
     MTQHIVSGGP QVVDSESFSA LTNVSRETLD RLLSYEALLR KWQKSINLVS NGSLPELWRR
     HMLDSAQLVC LVPESARRWI DLGSGGGFPG LVIAILLRER PGFQMHLVES DQRKCVFMRE
     VARVTGAPAT VHTVRIEAFA QGAEAGDVVS ARALAPLDRL FGWAAPLFGP ETIGLFLKGQ
     GLQDELTLAR ESWIFDAEFS PSQSDPEGSV LKVRGLHGPD GQPHRR