RSMG_THET8
ID RSMG_THET8 Reviewed; 249 AA.
AC Q9LCY2; Q5SGV9;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
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};
DE AltName: Full=Glucose-inhibited division protein B;
GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; Synonyms=gidB;
GN OrderedLocusNames=TTHA1971;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=11167017; DOI=10.1016/s0378-1119(00)00507-2;
RA Nardmann J., Messer W.;
RT "Identification and characterization of the dnaA upstream region of Thermus
RT thermophilus.";
RL Gene 261:299-303(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH AMP;
RP S-ADENOSYL-L-HOMOCYSTEINE AND S-ADENOSYL-L-METHIONINE, FUNCTION, DISRUPTION
RP PHENOTYPE, AND DISULFIDE BOND.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=19622680; DOI=10.1261/rna.1652709;
RA Gregory S.T., Demirci H., Belardinelli R., Monshupanee T., Gualerzi C.,
RA Dahlberg A.E., Jogl G.;
RT "Structural and functional studies of the Thermus thermophilus 16S rRNA
RT methyltransferase RsmG.";
RL RNA 15:1693-1704(2009).
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 527 of 16S rRNA. Shows a marked preference for deproteinized
CC 16S rRNA as substrate and is completely inactive with native 30S
CC subunits as substrate. {ECO:0000255|HAMAP-Rule:MF_00074,
CC ECO:0000269|PubMed:19622680}.
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 -!- DISRUPTION PHENOTYPE: Low-level streptomycin resistance.
CC {ECO:0000269|PubMed:19622680}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB89206.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ277593; CAB89206.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008226; BAD71794.1; -; Genomic_DNA.
DR RefSeq; WP_011229055.1; NC_006461.1.
DR RefSeq; YP_145237.1; NC_006461.1.
DR PDB; 3G88; X-ray; 1.87 A; A/B=1-249.
DR PDB; 3G89; X-ray; 1.50 A; A/B=1-249.
DR PDB; 3G8A; X-ray; 2.10 A; A/B/C/D/E/F=1-249.
DR PDB; 3G8B; X-ray; 2.10 A; A/B=1-249.
DR PDBsum; 3G88; -.
DR PDBsum; 3G89; -.
DR PDBsum; 3G8A; -.
DR PDBsum; 3G8B; -.
DR AlphaFoldDB; Q9LCY2; -.
DR SMR; Q9LCY2; -.
DR STRING; 300852.55773353; -.
DR EnsemblBacteria; BAD71794; BAD71794; BAD71794.
DR GeneID; 3169844; -.
DR KEGG; ttj:TTHA1971; -.
DR PATRIC; fig|300852.9.peg.1942; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_0_1_0; -.
DR OMA; ICFPHLH; -.
DR PhylomeDB; Q9LCY2; -.
DR BRENDA; 2.1.1.170; 2305.
DR EvolutionaryTrace; Q9LCY2; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Methyltransferase;
KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..249
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184358"
FT REGION 245..246
FT /note="RNA binding"
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 111..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 139..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT DISULFID 164..249
FT /evidence="ECO:0000269|PubMed:19622680"
FT CONFLICT 198..221
FT /note="ALERLGGRLGEVLALQLPLSGEAR -> LWSGSAGGLGRSSPSKLPSPGRRC
FT (in Ref. 1; CAB89206)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="T -> R (in Ref. 1; CAB89206)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3G88"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3G89"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3G89"
FT TURN 146..150
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3G89"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:3G89"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:3G89"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3G89"
SQ SEQUENCE 249 AA; 26832 MW; D346C3401D4A1619 CRC64;
MFHGKHPGGL SERGRALLLE GGKALGLDLK PHLEAFSRLY ALLQEASGKV NLTALRGEEE
VVVKHFLDSL TLLRLPLWQG PLRVLDLGTG AGFPGLPLKI VRPELELVLV DATRKKVAFV
ERAIEVLGLK GARALWGRAE VLAREAGHRE AYARAVARAV APLCVLSELL LPFLEVGGAA
VAMKGPRVEE ELAPLPPALE RLGGRLGEVL ALQLPLSGEA RHLVVLEKTA PTPPAYPRRP
GVPERHPLC
