RSMG_ACTPJ
ID RSMG_ACTPJ Reviewed; 205 AA.
AC B0BRY0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=APJL_1687;
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03;
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY70239.1; -; Genomic_DNA.
DR RefSeq; WP_005605652.1; NC_010278.1.
DR AlphaFoldDB; B0BRY0; -.
DR SMR; B0BRY0; -.
DR EnsemblBacteria; ABY70239; ABY70239; APJL_1687.
DR KEGG; apj:APJL_1687; -.
DR HOGENOM; CLU_065341_2_2_6; -.
DR OMA; ICFPHLH; -.
DR OrthoDB; 1590629at2; -.
DR Proteomes; UP000008547; 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..205
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000342902"
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 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ SEQUENCE 205 AA; 23267 MW; 1DBBF4608DA3F3A0 CRC64;
MRQKLDRLLE QAQINLTDQQ KEQLVGFVRL LDKWNKAYNL TSVRNPDEML VKHILDSLVV
SEHLQGNNFI DVGTGPGLPG IPLAIANPDK QFVLLDSLGK RITFIKNALR ELGITNVTPV
LSRVEEYKEQ TFDGVLSRAF ASLNDMVDWC YHLPNPQGKF YALKGIYAES EVQEIKNPIW
LEKVIPLSVP ELVGERHLVL LNKPN