ID   RSMC_ACIAD              Reviewed;         338 AA.
AC   Q6FE96;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=ACIAD0701;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67612.1; -; Genomic_DNA.
DR   RefSeq; WP_004922607.1; NC_005966.1.
DR   AlphaFoldDB; Q6FE96; -.
DR   SMR; Q6FE96; -.
DR   STRING; 62977.ACIAD0701; -.
DR   EnsemblBacteria; CAG67612; CAG67612; ACIAD0701.
DR   GeneID; 45233171; -.
DR   KEGG; aci:ACIAD0701; -.
DR   eggNOG; COG2813; Bacteria.
DR   HOGENOM; CLU_049581_0_0_6; -.
DR   OMA; RHCQLWQ; -.
DR   OrthoDB; 1027015at2; -.
DR   BioCyc; ASP62977:ACIAD_RS03215-MON; -.
DR   Proteomes; UP000000430; 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..338
FT                   /note="Ribosomal RNA small subunit methyltransferase C"
FT                   /id="PRO_0000369680"
SQ   SEQUENCE   338 AA;  38075 MW;  2600E347B91424AA CRC64;
     MDPRSEVVLR QQQYLAIKIL LINPPADELA QQLAHKHQVS VWTWNFADHQ YFQHQSIQSD
     FAVTFPDQIP DQVIIFVPKS KELLSYLLHV VVSHLPAGQH IFLVGEKKGG VERASKQLQS
     YGKTVKLDSA RHCQLWQTTI ETTEQLKPLE QWLKHYSVKN ENIQLEIYAL PGVFSQNHLD
     IGTAVLLPYL NQIKLGKIAD FGCGAGVISA YLAQLSPHNE IHALDIDAFA LRSTEFTFQR
     NGLASERLHL HAVTGIQDAP KALDVIVSNP PFHQGIHTDY SASEGLCKTA KQHLNTSGEL
     WIVANRFLNY PLLIEQTFGQ CQVKTDQQGF KILYAKAT