RSMC_ACIBC
ID RSMC_ACIBC Reviewed; 337 AA.
AC B2HYF8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=ACICU_03085;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(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; CP000863; ACC58397.1; -; Genomic_DNA.
DR RefSeq; WP_000371518.1; NZ_CP031380.1.
DR AlphaFoldDB; B2HYF8; -.
DR SMR; B2HYF8; -.
DR KEGG; abc:ACICU_03085; -.
DR HOGENOM; CLU_049581_0_0_6; -.
DR OMA; RHCQLWQ; -.
DR Proteomes; UP000008839; 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_0000369676"
SQ SEQUENCE 337 AA; 37521 MW; FE65AF5E428EBD88 CRC64;
MDPRSEVILR QHDYLKGRVL LINAPNDALV SQLPTEIDAS VWTWNYADYQ GFLNAGATAH
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
