RSMJ_ESCF3
ID RSMJ_ESCF3 Reviewed; 250 AA.
AC B7LSX8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=EFER_3490;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ90967.1; -; Genomic_DNA.
DR RefSeq; WP_000686614.1; NC_011740.1.
DR AlphaFoldDB; B7LSX8; -.
DR SMR; B7LSX8; -.
DR EnsemblBacteria; CAQ90967; CAQ90967; EFER_3490.
DR KEGG; efe:EFER_3490; -.
DR HOGENOM; CLU_076324_0_0_6; -.
DR OMA; SRYDIYP; -.
DR OrthoDB; 1696461at2; -.
DR BioCyc; EFER585054:EFER_RS17530-MON; -.
DR Proteomes; UP000000745; 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..250
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_1000198499"
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 250 AA; 26965 MW; 92FFD16796EA36D7 CRC64;
MKICLIDETG AGDGALSVLA SRWGLEHDED NLMALVLTPE HLELRKRDEP KLGGIFVDFV
GGTMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG RDAFVLASVG CRVRMLERNP
VVAALLDDGL ARGYADAEIG GWLQERLQLI HASSLTALTD ITPRPQVVYL DPMFPHKQKS
ALVKKEMRVF QSLVGPDLDA DGLLEPARLL ATKRVVVKRP DYAPPLANVA TPNAVVTKGH
RFDIYAGTPV