ID   RSMC_ESCF3              Reviewed;         343 AA.
AC   B7LNK6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=EFER_4412;
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 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; CU928158; CAQ91825.1; -; Genomic_DNA.
DR   RefSeq; WP_001272310.1; NC_011740.1.
DR   AlphaFoldDB; B7LNK6; -.
DR   SMR; B7LNK6; -.
DR   EnsemblBacteria; CAQ91825; CAQ91825; EFER_4412.
DR   KEGG; efe:EFER_4412; -.
DR   HOGENOM; CLU_049581_0_1_6; -.
DR   OMA; RHCQLWQ; -.
DR   OrthoDB; 1027015at2; -.
DR   BioCyc; EFER585054:EFER_RS22005-MON; -.
DR   Proteomes; UP000000745; 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; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..343
FT                   /note="Ribosomal RNA small subunit methyltransferase C"
FT                   /id="PRO_0000369716"
SQ   SEQUENCE   343 AA;  37684 MW;  6B7678734E8AF64C CRC64;
     MSAFTPASEV LLRHSDDFEQ SRILFAGDLQ DDLPARLDTA ASRAHTQQFH HWQVLSRQMG
     DNARFSLVAT ADDVADCDTL IYYWPKNKPE AQFQLMNLLS LLPVGTDIFV VGENRSGVRS
     AEQMLADYAP LNKVDSARRC GLYFGRLEKQ PMFDADKFWG EYNVDGLTVK TLPGVFSRDG
     LDVGSQLLLS TLTPHTKGKV LDVGCGAGVL SVAFARHSPK IRLTLCDVSA PAVEASRATL
     AANGIEGEVF ASNVFSEVKG RFDMIISNPP FHDGMQTSLD AAQTLIRGAV RHLNSGGELR
     IVANAFLPYP DVLDETFGFH EVIAQTGRFK VYRAIMTRQA KKG