RSMG_BORBU
ID RSMG_BORBU Reviewed; 208 AA.
AC P53363; O51197;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=BB_0177;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RA Old I.G.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=212;
RX PubMed=1490605; DOI=10.1016/0378-1097(92)90034-l;
RA Old I.G., Macdougall J.H., Saint-Girons I., Davidson B.E.;
RT "Mapping of genes on the linear chromosome of the bacterium Borrelia
RT burgdorferi: possible locations for its origin of replication.";
RL FEMS Microbiol. Lett. 78:245-250(1992).
CC -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC 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}.
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DR EMBL; X95668; CAA64969.1; -; Genomic_DNA.
DR EMBL; AJ003222; CAA06006.1; -; Genomic_DNA.
DR EMBL; X96434; CAA65297.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66558.1; -; Genomic_DNA.
DR EMBL; Z12160; CAA78150.1; -; Genomic_DNA.
DR PIR; A70122; A70122.
DR RefSeq; NP_212311.1; NC_001318.1.
DR RefSeq; WP_002665606.1; NC_001318.1.
DR AlphaFoldDB; P53363; -.
DR SMR; P53363; -.
DR STRING; 224326.BB_0177; -.
DR PRIDE; P53363; -.
DR EnsemblBacteria; AAC66558; AAC66558; BB_0177.
DR KEGG; bbu:BB_0177; -.
DR PATRIC; fig|224326.49.peg.574; -.
DR HOGENOM; CLU_065341_2_0_12; -.
DR OMA; IECELSN; -.
DR Proteomes; UP000001807; 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; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..208
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184225"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
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 101..103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 129..130
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"
FT CONFLICT 75..84
FT /note="LDVGSGAGFP -> PWTLEVVLDFR (in Ref. 1; CAA64969)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="S -> T (in Ref. 1; CAA64969/CAA06006)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="N -> S (in Ref. 1; CAA64969/CAA06006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 24177 MW; 7A65F11D86BDEF85 CRC64;
MISDIEFALS EHNFQFAYKD LQKINLYIKR ILLLNTRFNL ISNSNSNFNS ILNLHVIDSL
LGLSTVKEIN PSEVLDVGSG AGFPGIILAI FDSSRKYYLL ERSKKKSTFL KMIKLELDLE
NVKILEYEIE KEKKKYEFIT IRAFRNMNEY ALILKNLLKG GGLIMAYKGK FDRINLEVNQ
IKNLFSKIEV KSLNSKLRVD RNLVLLYR
