ID   RSMF_ECO24              Reviewed;         479 AA.
AC   A7ZMV8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 78.
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=EcE24377A_2064;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV19422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000800; ABV19422.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000057022.1; NC_009801.1.
DR   AlphaFoldDB; A7ZMV8; -.
DR   SMR; A7ZMV8; -.
DR   EnsemblBacteria; ABV19422; ABV19422; EcE24377A_2064.
DR   KEGG; ecw:EcE24377A_2064; -.
DR   HOGENOM; CLU_005316_6_2_6; -.
DR   Proteomes; UP000001122; 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_0000382570"
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