ID   RSMC_SHEON              Reviewed;         342 AA.
AC   Q8EIL1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000255|HAMAP-Rule:MF_01862};
DE            EC=2.1.1.172 {ECO:0000255|HAMAP-Rule:MF_01862};
DE   AltName: Full=16S rRNA m2G1207 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01862};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC {ECO:0000255|HAMAP-Rule:MF_01862};
GN   Name=rsmC {ECO:0000255|HAMAP-Rule:MF_01862}; OrderedLocusNames=SO_0828;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- FUNCTION: Specifically methylates the guanine in position 1207 of 16S
CC       rRNA in the 30S particle. {ECO:0000255|HAMAP-Rule:MF_01862}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42736, Rhea:RHEA-COMP:10213, Rhea:RHEA-COMP:10214,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.172;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01862};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01862}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01862}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.
CC       {ECO:0000255|HAMAP-Rule:MF_01862}.
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DR   EMBL; AE014299; AAN53904.2; -; Genomic_DNA.
DR   RefSeq; NP_716459.2; NC_004347.2.
DR   RefSeq; WP_011071121.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EIL1; -.
DR   SMR; Q8EIL1; -.
DR   STRING; 211586.SO_0828; -.
DR   PaxDb; Q8EIL1; -.
DR   KEGG; son:SO_0828; -.
DR   PATRIC; fig|211586.12.peg.795; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_049581_0_1_6; -.
DR   OrthoDB; 1027015at2; -.
DR   PhylomeDB; Q8EIL1; -.
DR   BioCyc; SONE211586:G1GMP-773-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052914; F:16S rRNA (guanine(1207)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01862; 16SrRNA_methyltr_C; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR013675; Mtase_sm_N.
DR   InterPro; IPR023543; rRNA_ssu_MeTfrase_C.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF08468; MTS_N; 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..342
FT                   /note="Ribosomal RNA small subunit methyltransferase C"
FT                   /id="PRO_0000369774"
SQ   SEQUENCE   342 AA;  37257 MW;  5100BBD79ABD8B5A CRC64;
     MLTNPSQVII RNQETLSQHK VLVLNHEADL LPKALLDVAS SVDALALDYH HYLHLAPQAN
     NKLRCYFGHQ LPHQNKYNTV IVYFPKAKPL APYLFNLAAQ HLVPNGQLLV VGENKGGIKS
     LVKLLPNYFA AGVKLDNARH SLLFGSSLID TAPEITLSDW ASQYQLSTPQ GNITICNLVG
     VFSEKHLDQG TELLLSHLPT LSGRVLDFGC GAGVIAATLL KAQPTLSLEC IDINAMALAS
     CELTLAANGM MAKVYPSDGL AQTSGKFDGI ISNPPFHDGL ASTTNIAQRF VADSAKQLQS
     KGIWQIVANR HLPYSDTIAA EFGQLTVPAE NNKYKLYYFQ QS