RSMA_THET8
ID RSMA_THET8 Reviewed; 271 AA.
AC Q5SM60;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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};
GN OrderedLocusNames=TTHA0083;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) IN COMPLEX WITH
RP 5'-DEOXY-5'-METHYLTHIOADENOSINE.
RX PubMed=19285505; DOI=10.1016/j.jmb.2009.02.066;
RA Demirci H., Belardinelli R., Seri E., Gregory S.T., Gualerzi C.,
RA Dahlberg A.E., Jogl G.;
RT "Structural rearrangements in the active site of the Thermus thermophilus
RT 16S rRNA methyltransferase KsgA in a binary complex with 5'-
RT methylthioadenosine.";
RL J. Mol. Biol. 388:271-282(2009).
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; AP008226; BAD69906.1; -; Genomic_DNA.
DR RefSeq; WP_011227698.1; NC_006461.1.
DR RefSeq; YP_143349.1; NC_006461.1.
DR PDB; 3FUT; X-ray; 1.52 A; A/B=1-271.
DR PDB; 3FUU; X-ray; 1.53 A; A=1-271.
DR PDB; 3FUV; X-ray; 1.95 A; A/B/C=1-271.
DR PDB; 3FUW; X-ray; 1.56 A; A=1-271.
DR PDB; 3FUX; X-ray; 1.68 A; A/B/C=1-271.
DR PDBsum; 3FUT; -.
DR PDBsum; 3FUU; -.
DR PDBsum; 3FUV; -.
DR PDBsum; 3FUW; -.
DR PDBsum; 3FUX; -.
DR AlphaFoldDB; Q5SM60; -.
DR SMR; Q5SM60; -.
DR STRING; 300852.55771465; -.
DR EnsemblBacteria; BAD69906; BAD69906; BAD69906.
DR GeneID; 3169411; -.
DR KEGG; ttj:TTHA0083; -.
DR PATRIC; fig|300852.9.peg.81; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_0_1_0; -.
DR OMA; KEEEPYF; -.
DR PhylomeDB; Q5SM60; -.
DR BRENDA; 2.1.1.182; 2305.
DR EvolutionaryTrace; Q5SM60; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..271
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000101631"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3FUU"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3FUT"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3FUV"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:3FUT"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3FUT"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3FUW"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3FUT"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3FUT"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:3FUT"
SQ SEQUENCE 271 AA; 29866 MW; 26B9BDCCAC8767B5 CRC64;
MSKLASPQSV RALLERHGLF ADKRFGQNFL VSEAHLRRIV EAARPFTGPV FEVGPGLGAL
TRALLEAGAE VTAIEKDLRL RPVLEETLSG LPVRLVFQDA LLYPWEEVPQ GSLLVANLPY
HIATPLVTRL LKTGRFARLV FLVQKEVAER MTARPKTPAY GVLTLRVAHH AVAERLFDLP
PGAFFPPPKV WSSLVRLTPT GALDDPGLFR LVEAAFGKRR KTLLNALAAA GYPKARVEEA
LRALGLPPRV RAEELDLEAF RRLREGLEGA V
