RSMJ_SHIFL
ID RSMJ_SHIFL Reviewed; 250 AA.
AC Q7UAV7; Q83J64;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SF3528, S4240;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of UPF0341 protein (YhiQ) from Shigella flexneri in
RT complex with S-adenosyl homocysteine, northeast structural genomics target
RT sfr275.";
RL Submitted (FEB-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN44984.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19202.1; -; Genomic_DNA.
DR RefSeq; NP_709277.2; NC_004337.2.
DR RefSeq; WP_000686608.1; NZ_WPGN01000102.1.
DR PDB; 2OYR; X-ray; 2.00 A; A=1-250.
DR PDBsum; 2OYR; -.
DR AlphaFoldDB; Q7UAV7; -.
DR SMR; Q7UAV7; -.
DR STRING; 198214.SF3528; -.
DR DNASU; 1080448; -.
DR EnsemblBacteria; AAN44984; AAN44984; SF3528.
DR EnsemblBacteria; AAP19202; AAP19202; S4240.
DR GeneID; 1026390; -.
DR GeneID; 58391087; -.
DR KEGG; sfl:SF3528; -.
DR KEGG; sfx:S4240; -.
DR PATRIC; fig|198214.7.peg.4153; -.
DR HOGENOM; CLU_076324_0_0_6; -.
DR OMA; SRYDIYP; -.
DR OrthoDB; 1696461at2; -.
DR EvolutionaryTrace; Q7UAV7; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..250
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_0000212093"
FT BINDING 101..102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 153..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|Ref.3"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:2OYR"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:2OYR"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2OYR"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:2OYR"
SQ SEQUENCE 250 AA; 26919 MW; 7826E98CBAC1C978 CRC64;
MKICLIDETG AGDGALSVLA ARWGLEHDED NLMALVLTPE HLELRKRDEP KLGGIFVDFV
GGAMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG RDAFVLASVG CRVRMLERNP
VVAALLDDGL ARGYADAEIG GWLQERLQLI HASSLTALTD ITPRPQVVYL DPMFPHKQKS
ALVKKEMRVF QSLVGPDLDA DGLLEPARLL ATKRVVVKRP DYAPPLANVA TPNAVVTKGH
RFDIYAGTPV