RSMA_RICBR
ID RSMA_RICBR Reviewed; 268 AA.
AC Q1RK29;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RBE_0204;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of ribosomal RNA small subunit methyltransferase A from
RT Rickettsia bellii determined by iodide SAD phasing.";
RL Submitted (MAY-2013) to the PDB data bank.
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; CP000087; ABE04285.1; -; Genomic_DNA.
DR RefSeq; WP_011476898.1; NC_007940.1.
DR PDB; 4JXJ; X-ray; 2.00 A; A=1-268.
DR PDBsum; 4JXJ; -.
DR AlphaFoldDB; Q1RK29; -.
DR SMR; Q1RK29; -.
DR STRING; 336407.RBE_0204; -.
DR PRIDE; Q1RK29; -.
DR EnsemblBacteria; ABE04285; ABE04285; RBE_0204.
DR KEGG; rbe:RBE_0204; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_0_1_5; -.
DR OMA; KEEEPYF; -.
DR OrthoDB; 2030110at2; -.
DR Proteomes; UP000001951; 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; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..268
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000257338"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4JXJ"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4JXJ"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:4JXJ"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4JXJ"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:4JXJ"
SQ SEQUENCE 268 AA; 29656 MW; 3122E85751E72C9D CRC64;
MLPSIAKHAA SHQIHPLKKH GQNFIFDGSL CDKIVRASGL EENSNVLEIG PGTGGLTRSI
LHKNPKLLTV IETDERCIPL LNEIKQYHPN LNIIKQDALK LKLSDLNTNK ITIISNLPYH
IGTELVIRWL KESSLVASMT LMLQKEVVER ICAKPSTKAY GRLSVICSLI ATVEKCFDVA
PTAFYPPPKV YSAIVKLTPL ENIPNSDLIS KVELITKMAF AGRRKMIKSS LKNLAPNISE
LLAKLNISDN CRAENLTPND YLSLASLI
