RSMC_YERPG
ID RSMC_YERPG Reviewed; 347 AA.
AC A9R058;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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};
GN OrderedLocusNames=YpAngola_A0840;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX86637.1; -; Genomic_DNA.
DR RefSeq; WP_002209206.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R058; -.
DR SMR; A9R058; -.
DR GeneID; 57974183; -.
DR KEGG; ypg:YpAngola_A0840; -.
DR PATRIC; fig|349746.12.peg.1792; -.
DR OMA; RHCQLWQ; -.
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..347
FT /note="Ribosomal RNA small subunit methyltransferase C"
FT /id="PRO_0000369802"
SQ SEQUENCE 347 AA; 37799 MW; CC2A77DDFEE54EFE CRC64;
MSALTPASEV ILRHSDEFIA RHVLFAGDLQ DALPAQFDAA GVRVHTNQYH HWQLLSNTLE
ENVQFGLLAT AETLAACDTL IYYWPKSKQE AQFQLANLLS ILPVGTDIFV VGENRSGVRS
AEEMLADFAQ LAKIDSARRC GLYHGRLDKQ PEFDADAWWE SYQVGGVTVK TLPGVFSRDS
LDSGSHLLLS TFNEPFKGSV LDVGCGAGVL ASVLAQQSPK IKWTLSDVSA AAIEASRATL
AVNNIEAQVI ASNVYSDIKG RFEMIISNPP FHDGIQTSLT AAEMLIRGAT AHLHVGGKLR
IVANSFLPYP ALLDAAFGSH EVLAQNGRFK VYQATVGRPP RDPKKKR