(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 129.
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}.
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   PDBsum; 6IFS; -.
DR   PDBsum; 6IFT; -.
DR   PDBsum; 6IFV; -.
DR   PDBsum; 6IFW; -.
DR   SMR; P37468; -.
DR   STRING; 224308.BSU00420; -.
DR   PaxDb; P37468; -.
DR   PRIDE; P37468; -.
DR   EnsemblBacteria; CAB11818; CAB11818; BSU00420.
DR   GeneID; 936358; -.
DR   KEGG; bsu:BSU00420; -.
DR   PATRIC; fig|224308.179.peg.42; -.
DR   eggNOG; ENOG4105D1X; Bacteria.
DR   eggNOG; COG0030; LUCA.
DR   HOGENOM; HOG000227962; -.
DR   InParanoid; P37468; -.
DR   KO; K02528; -.
DR   OMA; YYIATRL; -.
DR   PhylomeDB; P37468; -.
DR   BioCyc; BSUB:BSU00420-MONOMER; -.
DR   Proteomes; UP000001570; 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   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   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like.
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.
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;
DR   PRODOM; P37468.
DR   SWISS-2DPAGE; P37468.
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                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         31
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         56
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         77
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         102
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         127
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   STRAND          5..7
FT                   /evidence="ECO:0000244|PDB:6IFS"
FT   HELIX           8..18
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           19..21
FT                   /evidence="ECO:0000244|PDB:6IFS"
FT   HELIX           24..26
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           34..43
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          50..55
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   TURN            58..60
FT                   /evidence="ECO:0000244|PDB:6IFW"
FT   HELIX           61..69
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          71..77
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           82..89
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   TURN            90..92
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          94..101
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           103..105
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           108..115
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          120..127
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           130..132
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           133..142
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          148..155
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           156..162
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           173..181
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          182..190
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           192..194
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          195..197
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   STRAND          203..210
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           221..231
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   TURN            233..236
FT                   /evidence="ECO:0000244|PDB:6IFS"
FT   HELIX           239..246
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   TURN            248..252
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           254..263
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           272..274
FT                   /evidence="ECO:0000244|PDB:6IFT"
FT   HELIX           277..291
FT                   /evidence="ECO:0000244|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
//

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