RSMA_LEGPH
ID RSMA_LEGPH Reviewed; 256 AA.
AC Q5ZRF4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607};
DE EC=2.1.1.182 {ECO:0000255|HAMAP-Rule:MF_00607};
DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607};
DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607};
DE AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607};
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607};
GN Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607};
GN Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607}; OrderedLocusNames=lpg2928;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and
CC A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA
CC in the 30S particle. May play a critical role in biogenesis of 30S
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-
CC methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-
CC dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00607};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. RsmA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}.
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DR EMBL; AE017354; AAU28974.1; -; Genomic_DNA.
DR RefSeq; WP_010948613.1; NC_002942.5.
DR RefSeq; YP_096921.1; NC_002942.5.
DR AlphaFoldDB; Q5ZRF4; -.
DR SMR; Q5ZRF4; -.
DR STRING; 272624.lpg2928; -.
DR PaxDb; Q5ZRF4; -.
DR EnsemblBacteria; AAU28974; AAU28974; lpg2928.
DR GeneID; 66492103; -.
DR KEGG; lpn:lpg2928; -.
DR PATRIC; fig|272624.6.peg.3126; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_0_1_6; -.
DR OMA; KEEEPYF; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.100; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR011530; rRNA_adenine_dimethylase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00755; ksgA; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..256
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000101548"
FT BINDING 12
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 14
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
SQ SEQUENCE 256 AA; 28814 MW; DD237083943A063B CRC64;
MRHSPRKRFG QNFLQDKYII NEILRAINPL ADDNMLEIGP GLGALTQPLL QKLNQLTAIE
IDTDLQSYLT CLPASQGKLN LIPADALTVD FCQFGPHLRV VGNLPYNIST PLLIYLLKFI
TCIDDMHFML QKEVVERIAA AHGTKAYGRL SVMLQYHCEV EYLFDVPPEA FEPRPKVDSA
IVRLTPYRVS PFESVNTEKL ENIVAKAFAM RRKTLTNNLK GIISLSQLND LGIDGGKRPE
QISVAEYVQL AKFISN