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Database: UniProt
Entry: E6SVX5_BACT6
LinkDB: E6SVX5_BACT6
Original site: E6SVX5_BACT6 
ID   E6SVX5_BACT6            Unreviewed;       207 AA.
AC   E6SVX5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00074};
DE   AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
DE            Short=16S rRNA m7G methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
GN   Name=rsmG {ECO:0000256|HAMAP-Rule:MF_00074};
GN   OrderedLocusNames=Bache_2608 {ECO:0000313|EMBL:ADV44564.1};
OS   Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG
OS   15421 / P 36-108).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=693979 {ECO:0000313|EMBL:ADV44564.1, ECO:0000313|Proteomes:UP000008630};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P 36-108;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Bacteroides helcogenes P 36-108.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV44564.1, ECO:0000313|Proteomes:UP000008630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108
RC   {ECO:0000313|Proteomes:UP000008630};
RX   PubMed=21475586; DOI=10.4056/sigs.1513795;
RA   Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E.,
RA   Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT   "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT   108).";
RL   Stand. Genomic Sci. 4:45-53(2011).
CC   -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC       methyltransferase RsmG family. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00074}.
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DR   EMBL; CP002352; ADV44564.1; -; Genomic_DNA.
DR   RefSeq; WP_013548151.1; NC_014933.1.
DR   AlphaFoldDB; E6SVX5; -.
DR   STRING; 693979.Bache_2608; -.
DR   KEGG; bhl:Bache_2608; -.
DR   PATRIC; fig|693979.3.peg.2732; -.
DR   eggNOG; COG0357; Bacteria.
DR   HOGENOM; CLU_065341_2_2_10; -.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000008630; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR   InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00138; rsmG_gidB; 1.
DR   PANTHER; PTHR31760; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR31760:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF02527; GidB; 1.
DR   PIRSF; PIRSF003078; GidB; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00074};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074,
KW   ECO:0000313|EMBL:ADV44564.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008630};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_00074}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00074, ECO:0000313|EMBL:ADV44564.1}.
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         122..123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   207 AA;  23721 MW;  985FA5F28B62BCFD CRC64;
     MELILKYFPV LTEEQKKQYA ALYDLYLDWN SKINVISRKD IDNLYEHHVL HSLGIAQVIR
     FKPGTRIMDL GTGGGFPGIP LAILFPEVQF HLIDSIGKKI RVAEEVAGSI GLKNTTFRHA
     RAEEEKQTFD FVVSRAVMPL SDLMKIIRKN ISPKQQNALP NGLICLKGGE LAHEAMPLKN
     KTTMWDMKEF FEEDFFRTKK VVHVSNY
//
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