RSMG_BACSU
ID RSMG_BACSU Reviewed; 239 AA.
AC P25813;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=BSU41000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / CRK2000;
RX PubMed=1552862; DOI=10.1111/j.1365-2958.1992.tb01510.x;
RA Ogasawara N., Yoshikawa H.;
RT "Genes and their organization in the replication origin region of the
RT bacterial chromosome.";
RL Mol. Microbiol. 6:629-634(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=17573471; DOI=10.1128/jb.00558-07;
RA Nishimura K., Johansen S.K., Inaoka T., Hosaka T., Tokuyama S., Tahara Y.,
RA Okamoto S., Kawamura F., Douthwaite S., Ochi K.;
RT "Identification of the RsmG methyltransferase target as 16S rRNA nucleotide
RT G527 and characterization of Bacillus subtilis rsmG mutants.";
RL J. Bacteriol. 189:6068-6073(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "The 1.6 A crystal structure of Gram-positive Bacillus subtilis glucose
RT inhibited division protein b (gidB).";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 535 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074,
CC ECO:0000269|PubMed:17573471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- DISRUPTION PHENOTYPE: Low-level streptomycin resistance.
CC {ECO:0000269|PubMed:17573471}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
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DR EMBL; X62539; CAA44405.1; -; Genomic_DNA.
DR EMBL; D26185; BAA05230.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16137.1; -; Genomic_DNA.
DR PIR; I40441; BWBSGB.
DR RefSeq; NP_391980.1; NC_000964.3.
DR RefSeq; WP_003243029.1; NZ_JNCM01000034.1.
DR PDB; 1XDZ; X-ray; 1.60 A; A=1-239.
DR PDBsum; 1XDZ; -.
DR AlphaFoldDB; P25813; -.
DR SMR; P25813; -.
DR STRING; 224308.BSU41000; -.
DR PaxDb; P25813; -.
DR PRIDE; P25813; -.
DR DNASU; 937931; -.
DR EnsemblBacteria; CAB16137; CAB16137; BSU_41000.
DR GeneID; 937931; -.
DR KEGG; bsu:BSU41000; -.
DR PATRIC; fig|224308.179.peg.4442; -.
DR eggNOG; COG0357; Bacteria.
DR InParanoid; P25813; -.
DR OMA; ICFPHLH; -.
DR PhylomeDB; P25813; -.
DR BioCyc; BSUB:BSU41000-MON; -.
DR EvolutionaryTrace; P25813; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
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; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..239
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184215"
FT REGION 219..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 128..129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 19..38
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:1XDZ"
FT TURN 135..139
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:1XDZ"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1XDZ"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1XDZ"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1XDZ"
SQ SEQUENCE 239 AA; 26954 MW; 525826A929B32AA9 CRC64;
MNIEEFTSGL AEKGISLSPR QLEQFELYYD MLVEWNEKIN LTSITEKKEV YLKHFYDSIT
AAFYVDFNQV NTICDVGAGA GFPSLPIKIC FPHLHVTIVD SLNKRITFLE KLSEALQLEN
TTFCHDRAET FGQRKDVRES YDIVTARAVA RLSVLSELCL PLVKKNGLFV ALKAASAEEE
LNAGKKAITT LGGELENIHS FKLPIEESDR NIMVIRKIKN TPKKYPRKPG TPNKSPIEG
