RSMF_ECOLI
ID RSMF_ECOLI Reviewed; 479 AA.
AC P76273; O07980;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase F;
DE EC=2.1.1.178;
DE AltName: Full=16S rRNA m5C1407 methyltransferase;
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmF;
GN Name=rsmF; Synonyms=yebU; OrderedLocusNames=b1835, JW5301;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16678201; DOI=10.1016/j.jmb.2006.04.007;
RA Moeller Andersen N., Douthwaite S.;
RT "YebU is a m5C methyltransferase specific for 16 S rRNA nucleotide 1407.";
RL J. Mol. Biol. 359:777-786(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND CATALYTIC ACTIVITY.
RX PubMed=16793063; DOI=10.1016/j.jmb.2006.05.047;
RA Hallberg B.M., Ericsson U.B., Johnson K.A., Moeller Andersen N.,
RA Douthwaite S., Nordlund P., Beuscher A.E. IV, Erlandsen H.;
RT "The structure of the RNA m5C methyltransferase YebU from Escherichia coli
RT reveals a C-terminal RNA-recruiting PUA domain.";
RL J. Mol. Biol. 360:774-787(2006).
CC -!- FUNCTION: Specifically methylates the cytosine at position 1407
CC (m5C1407) of 16S rRNA. {ECO:0000269|PubMed:16678201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1407) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(1407) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42756, Rhea:RHEA-COMP:10223, Rhea:RHEA-COMP:10224,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.178;
CC Evidence={ECO:0000269|PubMed:16678201, ECO:0000269|PubMed:16793063};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000305}.
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DR EMBL; U00096; AAC74905.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15648.2; -; Genomic_DNA.
DR PIR; C64945; C64945.
DR RefSeq; NP_416349.2; NC_000913.3.
DR RefSeq; WP_001352260.1; NZ_SSZK01000001.1.
DR PDB; 2FRX; X-ray; 2.90 A; A/B/C/D=1-479.
DR PDBsum; 2FRX; -.
DR AlphaFoldDB; P76273; -.
DR SMR; P76273; -.
DR BioGRID; 4259158; 28.
DR STRING; 511145.b1835; -.
DR PaxDb; P76273; -.
DR PRIDE; P76273; -.
DR EnsemblBacteria; AAC74905; AAC74905; b1835.
DR EnsemblBacteria; BAA15648; BAA15648; BAA15648.
DR GeneID; 946348; -.
DR KEGG; ecj:JW5301; -.
DR KEGG; eco:b1835; -.
DR PATRIC; fig|511145.12.peg.1913; -.
DR EchoBASE; EB3777; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG3270; Bacteria.
DR HOGENOM; CLU_005316_6_2_6; -.
DR InParanoid; P76273; -.
DR OMA; PWCAEGF; -.
DR PhylomeDB; P76273; -.
DR BioCyc; EcoCyc:G7008-MON; -.
DR BioCyc; MetaCyc:G7008-MON; -.
DR BRENDA; 2.1.1.178; 2026.
DR EvolutionaryTrace; P76273; -.
DR PRO; PR:P76273; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01579; 16SrRNA_methyltr_F; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023545; rRNA_ssu_MeTfrase_F.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF13636; Methyltranf_PUA; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00446; nop2p; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 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..479
FT /note="Ribosomal RNA small subunit methyltransferase F"
FT /id="PRO_0000211822"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 125..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 215..235
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 236..247
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 295..299
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 355..368
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 381..391
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 399..405
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:2FRX"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:2FRX"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:2FRX"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:2FRX"
SQ SEQUENCE 479 AA; 53228 MW; 30D2B6AD01FCFF3E CRC64;
MAQHTVYFPD AFLTQMREAM PSTLSFDDFL AACQRPLRRS IRVNTLKISV ADFLQLTAPY
GWTLTPIPWC EEGFWIERDN EDALPLGSTA EHLSGLFYIQ EASSMLPVAA LFADGNAPQR
VMDVAAAPGS KTTQISARMN NEGAILANEF SASRVKVLHA NISRCGISNV ALTHFDGRVF
GAAVPEMFDA ILLDAPCSGE GVVRKDPDAL KNWSPESNQE IAATQRELID SAFHALRPGG
TLVYSTCTLN QEENEAVCLW LKETYPDAVE FLPLGDLFPG ANKALTEEGF LHVFPQIYDC
EGFFVARLRK TQAIPALPAP KYKVGNFPFS PVKDREAGQI RQAATGVGLN WDENLRLWQR
DKELWLFPVG IEALIGKVRF SRLGIKLAET HNKGYRWQHE AVIALASPDN MNAFELTPQE
AEEWYRGRDV YPQAAPVADD VLVTFQHQPI GLAKRIGSRL KNSYPRELVR DGKLFTGNA
