ID   C7BU50_PHOAA            Unreviewed;       247 AA.
AC   C7BU50;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000256|HAMAP-Rule:MF_01523};
DE            EC=2.1.1.242 {ECO:0000256|HAMAP-Rule:MF_01523};
DE   AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01523};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01523};
GN   Name=yhiQ {ECO:0000313|EMBL:CAQ82200.1};
GN   Synonyms=rsmJ {ECO:0000256|HAMAP-Rule:MF_01523};
GN   OrderedLocusNames=PAU_00107 {ECO:0000313|EMBL:CAQ82200.1};
OS   Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS   (Xenorhabdus luminescens (strain 2)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ82200.1, ECO:0000313|Proteomes:UP000002747};
RN   [1] {ECO:0000313|EMBL:CAQ82200.1, ECO:0000313|Proteomes:UP000002747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX   PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA   Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA   Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA   Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA   Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT   "Comparative genomics of the emerging human pathogen Photorhabdus
RT   asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL   BMC Genomics 10:302-302(2009).
CC   -!- FUNCTION: Specifically methylates the guanosine in position 1516 of 16S
CC       rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01523};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01523}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.
CC       {ECO:0000256|HAMAP-Rule:MF_01523}.
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DR   EMBL; FM162591; CAQ82200.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7BU50; -.
DR   STRING; 291112.PAU_00107; -.
DR   KEGG; pay:PAU_00107; -.
DR   eggNOG; COG0742; Bacteria.
DR   Proteomes; UP000002747; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 3.40.1630.10; YhiQ-like domain; 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; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE J; 1.
DR   PANTHER; PTHR36112:SF1; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE J; 1.
DR   Pfam; PF04445; SAM_MT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01523};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01523};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01523};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01523}; Transferase {ECO:0000256|HAMAP-Rule:MF_01523}.
FT   BINDING         101..102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01523"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01523"
FT   BINDING         153..154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01523"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01523"
SQ   SEQUENCE   247 AA;  27021 MW;  67E7FBDCCBCAD5AD CRC64;
     MDICLICEQG ADSSALSQLA KRWHLIHDES AVMALVLTPQ HLELRKLDEP KLGGIYVDFV
     SGVMAHRRRF GGGRGEAVAK AVGIKKDYLP TVVDATAGLG RDAFVLASLG CHVRMLERHP
     VVAALLDDGL QRGYQDAEIG GWLQERMTLL HASSITALVD ITPQPDVVYL DPMYPHKQKS
     ALVKKEMRVF QSLVGADEDA NHLLAPARAL AKRRVVVKRP DYAEPLAGVA ASAAITTKNH
     RFDIYPC
//