RSMF_ECO55
ID RSMF_ECO55 Reviewed; 479 AA.
AC B7L7N7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase F {ECO:0000255|HAMAP-Rule:MF_01579};
DE EC=2.1.1.178 {ECO:0000255|HAMAP-Rule:MF_01579};
DE AltName: Full=16S rRNA m5C1407 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01579};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmF {ECO:0000255|HAMAP-Rule:MF_01579};
GN Name=rsmF {ECO:0000255|HAMAP-Rule:MF_01579};
GN OrderedLocusNames=EC55989_2012;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Specifically methylates the cytosine at position 1407
CC (m5C1407) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01579}.
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:0000255|HAMAP-Rule:MF_01579};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01579}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|HAMAP-Rule:MF_01579}.
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DR EMBL; CU928145; CAU97871.1; -; Genomic_DNA.
DR RefSeq; WP_000057022.1; NC_011748.1.
DR AlphaFoldDB; B7L7N7; -.
DR SMR; B7L7N7; -.
DR EnsemblBacteria; CAU97871; CAU97871; EC55989_2012.
DR KEGG; eck:EC55989_2012; -.
DR HOGENOM; CLU_005316_6_2_6; -.
DR OMA; PWCAEGF; -.
DR Proteomes; UP000000746; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..479
FT /note="Ribosomal RNA small subunit methyltransferase F"
FT /id="PRO_1000185641"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 125..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
SQ SEQUENCE 479 AA; 53179 MW; 51D71E76D2617F5A CRC64;
MAQHTVYFPD AFLTQMREAM PSTLSFDDFL AACQRPLRRS IRVNTLKISV ADFLQLTAPY
GWTLTPIPWC EEGFWIERDN EDALPLGSTA EHLSGLFYIQ EASSMLPVAA LFADDNAPQR
VMDVAAAPGS KTTQIAARMN NEGAILANEF SASRVKVLHA NISRCGISNV ALTHFDGRVF
GAAVPEMFDA ILLDAPCSGE GVVRKDPDAL KNWSPESNQE IAATQRELID SAFHALRPGG
TLVYSTCTLN QEENEAVCLW LKETYPDAVE FLPLGDLFPG ANKALTEEGF LHVFPQIYDC
EGFFVARLRK TQAIPALPAP KYKVGNFPFS PVKDREAGQI RQAAASVGLN WDGNLRLWQR
DKELWLFPVG IEALIGKVRF SRLGIKLAET HNKGYRWQHE AVIALATPDN VNAFELTPQE
AEEWYRGRDV YPQAAPVADD VLVTFQHQPI GLAKRIGSRL KNSYPRELVR DGKLFTGNA
