RSMG_CROS8
ID RSMG_CROS8 Reviewed; 207 AA.
AC A7MMW2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=ESA_04014;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU79200.1; -; Genomic_DNA.
DR RefSeq; WP_012126196.1; NC_009778.1.
DR AlphaFoldDB; A7MMW2; -.
DR SMR; A7MMW2; -.
DR EnsemblBacteria; ABU79200; ABU79200; ESA_04014.
DR GeneID; 56732654; -.
DR KEGG; esa:ESA_04014; -.
DR PATRIC; fig|290339.8.peg.3562; -.
DR HOGENOM; CLU_065341_2_2_6; -.
DR OMA; ICFPHLH; -.
DR OrthoDB; 1590629at2; -.
DR Proteomes; UP000000260; 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..207
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_1000010143"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
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 124..125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ SEQUENCE 207 AA; 23242 MW; F6A4FAC6A01852C2 CRC64;
MLNTLTRLLD DAGITLPEHQ KAQLVAYVDM LNKWNKAYNL TSVRDPNEML VRHIMDSIVV
EPHLKGTRFI DVGTGPGLPG IPLAIVRPDS HFTLLDSLGK RVRFLRQVQH ELKLDNITPV
QSRVEAFPAE PPFDGVISRA FASLSDMVNW CHHLPGEEGR FYALKGQRPD DEISALPSGF
AVEEIVRLSV PRLDGERHLV ILKANRT