ID   RSMJ_HAEIN              Reviewed;         257 AA.
AC   P44901;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   03-AUG-2022, entry version 101.
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}; OrderedLocusNames=HI_0849;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22506.1; ALT_INIT; Genomic_DNA.
DR   PIR; I64159; I64159.
DR   RefSeq; NP_439009.1; NC_000907.1.
DR   RefSeq; WP_005693198.1; NC_000907.1.
DR   AlphaFoldDB; P44901; -.
DR   SMR; P44901; -.
DR   STRING; 71421.HI_0849; -.
DR   DNASU; 949861; -.
DR   EnsemblBacteria; AAC22506; AAC22506; HI_0849.
DR   KEGG; hin:HI_0849; -.
DR   PATRIC; fig|71421.8.peg.890; -.
DR   eggNOG; COG0742; Bacteria.
DR   HOGENOM; CLU_076324_0_0_6; -.
DR   PhylomeDB; P44901; -.
DR   BioCyc; HINF71421:G1GJ1-889-MON; -.
DR   Proteomes; UP000000579; 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; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..257
FT                   /note="Ribosomal RNA small subunit methyltransferase J"
FT                   /id="PRO_0000212069"
FT   BINDING         107..108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT   BINDING         123..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
SQ   SEQUENCE   257 AA;  28549 MW;  7B63FEF72989D941 CRC64;
     MAHSQVGIQL ISESTEKTLA ELIALCAEHN IIHNEKSPLA LVQTDDRLEL RKLDEPKLGA
     VYVDFVGGTM AHRRKFGGGR GEAVAKAVGI KGSALPTVID ATAGLGRDAF VLAAIGCQVR
     LVERHPVVFL LLQDGLNRAY QDEEIGEMLQ QNLHLLNVQH INELDPNSDY ADVVYLDPMY
     PHKQKSALVK KEMRVFQHLV GADLDADELL LPALQLAKKR VVVKRPDYAE FLCGKQPHFS
     HETKNHRFDI YMGASQC