ID   RSMJ_VIBCH              Reviewed;         261 AA.
AC   Q9KVR6;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 85.
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=VC_0073;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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=AAF93251.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93251.1; ALT_INIT; Genomic_DNA.
DR   PIR; A82368; A82368.
DR   RefSeq; NP_229732.2; NC_002505.1.
DR   RefSeq; WP_000908213.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KVR6; -.
DR   SMR; Q9KVR6; -.
DR   STRING; 243277.VC_0073; -.
DR   DNASU; 2614881; -.
DR   EnsemblBacteria; AAF93251; AAF93251; VC_0073.
DR   GeneID; 57741421; -.
DR   KEGG; vch:VC_0073; -.
DR   PATRIC; fig|243277.26.peg.71; -.
DR   eggNOG; COG0742; Bacteria.
DR   HOGENOM; CLU_076324_0_0_6; -.
DR   OMA; SRYDIYP; -.
DR   Proteomes; UP000000584; Chromosome 1.
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..261
FT                   /note="Ribosomal RNA small subunit methyltransferase J"
FT                   /id="PRO_0000212094"
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         176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
SQ   SEQUENCE   261 AA;  28745 MW;  FFC431D001E71DD1 CRC64;
     MLIQLICQAP QRAQELEQIA ARWQLQASDD SPFALVLSEE RLELRKLDEP KLGAIYVDWV
     EGAVAHRRKF GGGKGQSIAK AAGLNKGVTP VVLDATAGLG RDAFVLASLG CRVQMVERHP
     VVAALLEDGL QRAKQDDEIG AWVSERISLL HASSHDALQQ LASDPNFTSP DVVYLDPMYP
     HPENKKKTAL VKKEMRVFQS LVGADNDADA LLEPALQLAQ KRVVVKRPDY APWLGNRKPS
     MAMETKKNRF DVYVIAAMSG E