RSMJ_SALCH
ID RSMJ_SALCH Reviewed; 252 AA.
AC Q57IN4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523};
DE EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523};
DE AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
GN Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523}; Synonyms=yhiQ;
GN OrderedLocusNames=SCH_3522;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
CC -!- FUNCTION: Specifically methylates the guanosine in position 1516 of 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412, Rhea:RHEA-COMP:10413,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.242;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01523};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.
CC {ECO:0000255|HAMAP-Rule:MF_01523}.
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DR EMBL; AE017220; AAX67428.1; -; Genomic_DNA.
DR RefSeq; WP_001165128.1; NC_006905.1.
DR AlphaFoldDB; Q57IN4; -.
DR SMR; Q57IN4; -.
DR EnsemblBacteria; AAX67428; AAX67428; SCH_3522.
DR KEGG; sec:SCH_3522; -.
DR HOGENOM; CLU_076324_0_0_6; -.
DR OMA; SRYDIYP; -.
DR Proteomes; UP000000538; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR36112; PTHR36112; 1.
DR Pfam; PF04445; SAM_MT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..252
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_0000212088"
FT BINDING 101..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 153..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
SQ SEQUENCE 252 AA; 27268 MW; 908A94C42EACA056 CRC64;
MQICLMDETG ATDGALSVLA ARWGLEHDED NPMALVLTPQ HLELRKRDEP KLGGIFVDFV
GGAMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG RDAFVLASVG CRVRMLERNP
VVAALLDDGL TRGYADADIG GWLQERLQLI HASSLTALTD ITPRPQVVYL DPMFPHRQKS
ALVKKEMRVF QSLVGPDLDA DGLLEPARQL ATKRVVVKRP DYAPPLADVA TPNAVVTKGH
RFDIYAGTPL TE