ID   RSMC_ECO45              Reviewed;         343 AA.
AC   B7MNC1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=ECS88_4992;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928161; CAR06134.1; -; Genomic_DNA.
DR   RefSeq; WP_001272330.1; NC_011742.1.
DR   AlphaFoldDB; B7MNC1; -.
DR   SMR; B7MNC1; -.
DR   EnsemblBacteria; CAR06134; CAR06134; ECS88_4992.
DR   KEGG; ecz:ECS88_4992; -.
DR   HOGENOM; CLU_049581_0_1_6; -.
DR   OMA; RHCQLWQ; -.
DR   Proteomes; UP000000747; 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_0000369709"
SQ   SEQUENCE   343 AA;  37625 MW;  81E190CB86E4BAC2 CRC64;
     MSAFTPASEV LLRHSDDFEQ SRILFAGDLQ DDLPARLDTA ASRAHTQQFH HWQVLSRQMG
     DNARFSLVAT ADDVADCDTL IYYWPKNKPE AQFQLMNLLS LLPVGTDIFV VGENRSGVRS
     AEQMLADYAP LNKVDSARRC GLYFGRLEKQ PVFDAEKFWG EYSVDGLTVK TLPGVFSRDG
     LDVGSQLLLS TLTPHTKGKV LDVGCGAGVL SVAFARHSPK IRLTLCDVSA PAVEASRATL
     AANGVEGEVF ASNVFSEVKG RFDMIISNPP FHDGMQTSLD AAQTLIRGAV RHLNSGGELR
     IVANAFLPYP DVLDETFGFH EVIAQTGRFK VYRAIMTRQA KKG