(data stored in SCRATCH zone)

SWISSPROT: RSME_BACSU

ID   RSME_BACSU              Reviewed;         256 AA.
AC   P54461;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase E;
DE            EC=2.1.1.193;
DE   AltName: Full=16S rRNA m3U1498 methyltransferase;
GN   Name=rsmE; Synonyms=yqeU; OrderedLocusNames=BSU25440;
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 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=9023197; DOI=10.1128/jb.179.4.1153-1164.1997;
RA   Homuth G., Masuda S., Mogk A., Kobayashi Y., Schumann W.;
RT   "The dnaK operon of Bacillus subtilis is heptacistronic.";
RL   J. Bacteriol. 179:1153-1164(1997).
RN   [3]
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   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-256.
RX   PubMed=16021622; DOI=10.1002/prot.20541;
RA   Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA   Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA   Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA   Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA   Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA   Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA   Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA   Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA   Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT   "Structural analysis of a set of proteins resulting from a bacterial
RT   genomics project.";
RL   Proteins 60:787-796(2005).
CC   -!- FUNCTION: Specifically methylates the N3 position of the uracil ring of
CC       uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S
CC       ribosomal subunit (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) +
CC         N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42920, Rhea:RHEA-COMP:10283, Rhea:RHEA-COMP:10284,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74502; EC=2.1.1.193;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family.
CC       {ECO:0000305}.
DR   EMBL; D84432; BAA12467.1; -; Genomic_DNA.
DR   EMBL; D83717; BAA12079.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14486.1; -; Genomic_DNA.
DR   PIR; D69952; D69952.
DR   RefSeq; NP_390422.1; NC_000964.3.
DR   RefSeq; WP_003230015.1; NZ_JNCM01000036.1.
DR   PDB; 1VHK; X-ray; 2.60 A; A/B/C/D=2-256.
DR   PDBsum; 1VHK; -.
DR   SMR; P54461; -.
DR   STRING; 224308.BSU25440; -.
DR   PaxDb; P54461; -.
DR   PRIDE; P54461; -.
DR   EnsemblBacteria; CAB14486; CAB14486; BSU25440.
DR   GeneID; 937856; -.
DR   KEGG; bsu:BSU25440; -.
DR   PATRIC; fig|224308.179.peg.2765; -.
DR   eggNOG; ENOG4107TVK; Bacteria.
DR   eggNOG; COG1385; LUCA.
DR   HOGENOM; HOG000015265; -.
DR   InParanoid; P54461; -.
DR   KO; K09761; -.
DR   OMA; ERMEFTI; -.
DR   PhylomeDB; P54461; -.
DR   BioCyc; BSUB:BSU25440-MONOMER; -.
DR   EvolutionaryTrace; P54461; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR006700; rRNA_ssu_MeTrfase-E.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR30027; PTHR30027; 1.
DR   Pfam; PF04452; Methyltrans_RNA; 1.
DR   PIRSF; PIRSF015601; MTase_slr0722; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00046; TIGR00046; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54461.
DR   SWISS-2DPAGE; P54461.
KW   3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..256
FT                   /note="Ribosomal RNA small subunit methyltransferase E"
FT                   /id="PRO_0000176205"
FT   STRAND          3..5
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           10..14
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          15..23
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           24..30
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   TURN            31..33
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          40..44
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          50..58
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          60..70
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          78..86
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           92..102
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          107..111
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           122..127
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           129..142
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           157..163
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           164..166
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          167..173
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           185..191
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          198..203
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           211..219
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   STRAND          223..225
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   TURN            234..236
FT                   /evidence="ECO:0000244|PDB:1VHK"
FT   HELIX           237..250
FT                   /evidence="ECO:0000244|PDB:1VHK"
SQ   SEQUENCE   256 AA;  28802 MW;  AAE708FE4283157E CRC64;
     MQRYFIELTK QQIEEAPTFS ITGEEVHHIV NVMRMNEGDQ IICCSQDGFE AKCELQSVSK
     DKVSCLVIEW TNENRELPIK VYIASGLPKG DKLEWIIQKG TELGAHAFIP FQAARSVVKL
     DDKKAKKKRE RWTKIAKEAA EQSYRNEVPR VMDVHSFQQL LQRMQDFDKC VVAYEESSKQ
     GEISAFSAIV SSLPKGSSLL IVFGPEGGLT EAEVERLTEQ DGVTCGLGPR ILRTETAPLY
     ALSAISYQTE LLRGDQ
//

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