RSMC_ACIBS
ID RSMC_ACIBS Reviewed; 337 AA.
AC B0VRJ4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=ABSDF0610;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAO99988.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VRJ4; -.
DR SMR; B0VRJ4; -.
DR EnsemblBacteria; CAO99988; CAO99988; ABSDF0610.
DR KEGG; abm:ABSDF0610; -.
DR HOGENOM; CLU_049581_0_0_6; -.
DR OMA; RHCQLWQ; -.
DR Proteomes; UP000001741; 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..337
FT /note="Ribosomal RNA small subunit methyltransferase C"
FT /id="PRO_0000369679"
SQ SEQUENCE 337 AA; 37554 MW; 7CD872F21AF9415B CRC64;
MDPRSEVILR QQDYLKGRVL LINAPNDALV SQLPTEIDAS VWTWNYADYQ VFLNAGATAH
FSVEFPLQEF DQAIIFVPKS KELLNYILHV VMSHLKIDQS VFLVGEKKGG VERAAKQLQS
FGKILKLDSA RHCQLWHLKI EKTEKIKPLE SWLKTYTVQV NEQELTICAL PGVFSQTHLD
VGTAVLLPYL NQVKSGRIAD FGCGAGIISC YLAKANSSNI IHALDIDAFA LQSTEMTFSR
NGIGSDQLRL QPVTGIADAP TELDAIVSNP PFHQGIHTNY DASEGLCQNA KKHLKASGEL
WIVANRFLNY PILIEKHFGQ CEIKTDLQGF KVLYACA
