ID   RSMF_ECO45              Reviewed;         479 AA.
AC   B7MBP2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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}; OrderedLocusNames=ECS88_1888;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
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; CU928161; CAR03194.1; -; Genomic_DNA.
DR   RefSeq; WP_001350670.1; NC_011742.1.
DR   AlphaFoldDB; B7MBP2; -.
DR   SMR; B7MBP2; -.
DR   EnsemblBacteria; CAR03194; CAR03194; ECS88_1888.
DR   KEGG; ecz:ECS88_1888; -.
DR   HOGENOM; CLU_005316_6_2_6; -.
DR   OMA; PWCAEGF; -.
DR   Proteomes; UP000000747; 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_1000147564"
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;  53238 MW;  4FD26BEDB12E2346 CRC64;
     MAQHTVYFPD AFLTQMREAM PSTLSFDDFL AACQRPLRRS IRVNTLKTSV ADFLQLTAPY
     GWTLTPIPWC EEGFWIERDS EDALPLGSTA EHLSGLFYIQ EASSMLPVAA LFADGNAPQR
     VMDVAAAPGS KTTQIAARMN NKGAILANEF SASRVKVLHA NISRCGISNV ALTHFDGRVF
     GAAVPEMFDA ILLDAPCSGE GVVRKDPDAL KNWSPESNQE IAATQRELID SAFHALRLGG
     TLVYSTCTLN REENEAVCLW LKETYHDAVE FLPLGDLFPG ANKALTEDGF LHVFPQIYDC
     EGFFVARLRK TQAIPVLPAP KYKVGNFPFS PVKDREAGQI RQAAASVGLN WDENLRLWQR
     DKELWLFPVG IEALIGKVRF SRLGIKLAET HNKGYRWQHE AVIALASPDN VNAFELTPQE
     AEEWYRGRDV YPQAAPVADD VLVTFQHQPI GLAKRIGSRL KNSYPRELVR DGKLFTGNA