RSMJ_SALTY
ID RSMJ_SALTY Reviewed; 252 AA.
AC Q9X6G2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=STM3593;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=10629202; DOI=10.1128/jb.182.2.518-521.2000;
RA Conlin C.A., Miller C.G.;
RT "opdA, a Salmonella enterica serovar Typhimurium gene encoding a protease,
RT is part of an operon regulated by heat shock.";
RL J. Bacteriol. 182:518-521(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of UPF0341 protein YhiQ from Salmonella typhimurium.";
RL Submitted (APR-2007) to the PDB data bank.
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; AF137028; AAD31478.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22453.1; -; Genomic_DNA.
DR RefSeq; NP_462494.1; NC_003197.2.
DR RefSeq; WP_001165134.1; NC_003197.2.
DR PDB; 2PKW; X-ray; 2.10 A; A=1-252.
DR PDBsum; 2PKW; -.
DR AlphaFoldDB; Q9X6G2; -.
DR SMR; Q9X6G2; -.
DR STRING; 99287.STM3593; -.
DR PaxDb; Q9X6G2; -.
DR DNASU; 1255116; -.
DR EnsemblBacteria; AAL22453; AAL22453; STM3593.
DR GeneID; 1255116; -.
DR KEGG; stm:STM3593; -.
DR PATRIC; fig|99287.12.peg.3797; -.
DR HOGENOM; CLU_076324_0_0_6; -.
DR OMA; SRYDIYP; -.
DR PhylomeDB; Q9X6G2; -.
DR BioCyc; SENT99287:STM3593-MON; -.
DR EvolutionaryTrace; Q9X6G2; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..252
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_0000212091"
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"
FT CONFLICT 225
FT /note="P -> PP (in Ref. 1; AAD31478)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2PKW"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2PKW"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:2PKW"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2PKW"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:2PKW"
SQ SEQUENCE 252 AA; 27300 MW; 3037E3B43E070046 CRC64;
MQICLMDETG ATDGALSVLA ARWGLEHDED NPMALVMTPQ HLELRKRDEP KLGGIFVDFV
GGAMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG RDAFVLASVG CRVRMLERNP
VVAALLDDGL TRGYADADIG GWLQERLQLI HASSLTALTD ITPRPQVVYL DPMFPHRQKS
ALVKKEMRVF QSLVGPDLDA DGLLEPARQL ATKRVVVKRP DYAPPLADVA TPNAIVTKGH
RFDIYAGTPL TE
