ID   RSMF_PHOPR              Reviewed;         476 AA.
AC   Q6LQU5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
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=PBPRA1927;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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=CAG20331.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR378669; CAG20331.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041394298.1; NC_006370.1.
DR   AlphaFoldDB; Q6LQU5; -.
DR   SMR; Q6LQU5; -.
DR   STRING; 298386.PBPRA1927; -.
DR   EnsemblBacteria; CAG20331; CAG20331; PBPRA1927.
DR   KEGG; ppr:PBPRA1927; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   HOGENOM; CLU_005316_6_2_6; -.
DR   OrthoDB; 1064993at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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; 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; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..476
FT                   /note="Ribosomal RNA small subunit methyltransferase F"
FT                   /id="PRO_0000285002"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         124..130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
SQ   SEQUENCE   476 AA;  53325 MW;  E5BE7D197FC659CD CRC64;
     MNPKTYIPDT FIEMIREIMP EHLSMDEFIA SCRTPLRRSI RVNTLKISVE DFLVRVSDKD
     WTLTPVPWCD TGFWIEREDE KSVSLGNTAE HMAGLFYIQE ASSMMPVTAL LKNNDALDCV
     LDMASAPGSK TTQIACAMQN RGVLVANELA ASRIKVLHAN LQRCGVYNAA LTHFDGCVFG
     GWAPESFDTI LLDAPCSGEG AIRKDGDAMA NWSLSSIEDI AAIQRNLIIS AFQALKTGGM
     MVYSTCTLNL SENQHVCHFL KETFGDAVEF EPLGDLFEGA EKSLTEDGFL HVYPQIFDSE
     GFFVARIRKH AAVETPKVKK RMGKFPFTIV ADADKAIIAE QLQATLSITL PAESDVWVRE
     KEVWLFPANL RPLIGEIRFQ RMGVKLAEQH KKGYRWQHEA VMTLATGKED VAIDLAPEQA
     KEWFMGRDIR PENLLGKGEV VVTYRDYPIG IGKWVGNRIK NGLPRELVRD TNLFDI