RSMA_BACSU
ID RSMA_BACSU Reviewed; 292 AA.
AC P37468;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=BSU00420;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11233981; DOI=10.1017/s1355838201002163;
RA Condon C., Brechemier-Baey D., Beltchev B., Grunberg-Manago M., Putzer H.;
RT "Identification of the gene encoding the 5S ribosomal RNA maturase in
RT Bacillus subtilis: mature 5S rRNA is dispensable for ribosome function.";
RL RNA 7:242-253(2001).
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 -!- DISRUPTION PHENOTYPE: No visible phenotype. Not essential.
CC {ECO:0000269|PubMed:11233981}.
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; D26185; BAA05277.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11818.1; -; Genomic_DNA.
DR PIR; S66071; S66071.
DR RefSeq; NP_387923.1; NC_000964.3.
DR RefSeq; WP_003226751.1; NZ_JNCM01000028.1.
DR PDB; 6IFS; X-ray; 2.27 A; A/B=1-292.
DR PDB; 6IFT; X-ray; 1.90 A; A=1-292.
DR PDB; 6IFV; X-ray; 3.11 A; A/B=1-215.
DR PDB; 6IFW; X-ray; 2.95 A; A/B=27-292.
DR PDB; 7V2L; EM; 3.30 A; W=1-292.
DR PDB; 7V2M; EM; 3.40 A; U/W=1-292.
DR PDB; 7V2N; EM; 3.60 A; U=1-292.
DR PDB; 7V2O; EM; 3.50 A; U=1-292.
DR PDB; 7V2P; EM; 3.30 A; U=1-292.
DR PDB; 7V2Q; EM; 3.24 A; U/W=1-292.
DR PDBsum; 6IFS; -.
DR PDBsum; 6IFT; -.
DR PDBsum; 6IFV; -.
DR PDBsum; 6IFW; -.
DR PDBsum; 7V2L; -.
DR PDBsum; 7V2M; -.
DR PDBsum; 7V2N; -.
DR PDBsum; 7V2O; -.
DR PDBsum; 7V2P; -.
DR PDBsum; 7V2Q; -.
DR AlphaFoldDB; P37468; -.
DR SMR; P37468; -.
DR STRING; 224308.BSU00420; -.
DR PaxDb; P37468; -.
DR PRIDE; P37468; -.
DR EnsemblBacteria; CAB11818; CAB11818; BSU_00420.
DR GeneID; 936358; -.
DR KEGG; bsu:BSU00420; -.
DR PATRIC; fig|224308.179.peg.42; -.
DR eggNOG; COG0030; Bacteria.
DR InParanoid; P37468; -.
DR OMA; KEEEPYF; -.
DR PhylomeDB; P37468; -.
DR BioCyc; BSUB:BSU00420-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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..292
FT /note="Ribosomal RNA small subunit methyltransferase A"
FT /id="PRO_0000101485"
FT BINDING 29
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6IFS"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6IFS"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:6IFT"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6IFW"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:6IFT"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6IFT"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:6IFT"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:6IFS"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:6IFT"
FT TURN 248..252
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6IFT"
FT HELIX 277..291
FT /evidence="ECO:0007829|PDB:6IFT"
SQ SEQUENCE 292 AA; 32721 MW; 26CE063F33BA8994 CRC64;
MNKDIATPIR TKEILKKYGF SFKKSLGQNF LIDTNILNRI VDHAEVTEKT GVIEIGPGIG
ALTEQLAKRA KKVVAFEIDQ RLLPILKDTL SPYENVTVIH QDVLKADVKS VIEEQFQDCD
EIMVVANLPY YVTTPIIMKL LEEHLPLKGI VVMLQKEVAE RMAADPSSKE YGSLSIAVQF
YTEAKTVMIV PKTVFVPQPN VDSAVIRLIL RDGPAVDVEN ESFFFQLIKA SFAQRRKTLL
NNLVNNLPEG KAQKSTIEQV LEETNIDGKR RGESLSIEEF AALSNGLYKA LF
