RSME_HAEIN
ID RSME_HAEIN Reviewed; 245 AA.
AC P44627;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
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; OrderedLocusNames=HI_0303;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-245, AND IDENTIFICATION AS
RP PUTATIVE RNA METHYLTRANSFERASE.
RX PubMed=14517985; DOI=10.1002/prot.10510;
RA Forouhar F., Shen J., Xiao R., Acton T.B., Montelione G.T., Tong L.;
RT "Functional assignment based on structural analysis: crystal structure of
RT the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA
RT methyltransferase with a deep trefoil knot.";
RL Proteins 53:329-332(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-245.
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}.
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DR EMBL; L42023; AAC21968.1; -; Genomic_DNA.
DR PIR; D64147; D64147.
DR RefSeq; NP_438470.1; NC_000907.1.
DR RefSeq; WP_005694361.1; NC_000907.1.
DR PDB; 1NXZ; X-ray; 2.00 A; A/B=2-245.
DR PDB; 1VHY; X-ray; 1.90 A; A/B=2-245.
DR PDBsum; 1NXZ; -.
DR PDBsum; 1VHY; -.
DR AlphaFoldDB; P44627; -.
DR SMR; P44627; -.
DR STRING; 71421.HI_0303; -.
DR EnsemblBacteria; AAC21968; AAC21968; HI_0303.
DR KEGG; hin:HI_0303; -.
DR PATRIC; fig|71421.8.peg.320; -.
DR eggNOG; COG1385; Bacteria.
DR HOGENOM; CLU_067442_5_1_6; -.
DR OMA; TQWKGER; -.
DR PhylomeDB; P44627; -.
DR BioCyc; HINF71421:G1GJ1-321-MON; -.
DR EvolutionaryTrace; P44627; -.
DR Proteomes; UP000000579; 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;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..245
FT /note="Ribosomal RNA small subunit methyltransferase E"
FT /id="PRO_0000176202"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 45..57
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1NXZ"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:1VHY"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:1VHY"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1VHY"
SQ SEQUENCE 245 AA; 27373 MW; 1F6BEA83A791328C CRC64;
MRIPRIYHPI SLENQTQCYL SEDAANHVAR VLRMTEGEQL ELFDGSNHIY PAKIIESNKK
SVKVEILGRE LADKESHLKI HLGQVISRGE RMEFTIQKSV ELGVNVITPL WSERCGVKLD
AERMDKKIQQ WQKIAIAACE QCGRNIVPEI RPLMKLQDWC AENDGALKLN LHPRAHYSIK
TLPTIPAGGV RLLIGSEGGL SAQEIAQTEQ QGFTEILLGK RVLRTETASL AAISALQICF
GDLGE
