RSMF_SERP5
ID RSMF_SERP5 Reviewed; 478 AA.
AC A8GDM6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
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=Spro_2113;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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=ABV41216.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000826; ABV41216.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041418930.1; NC_009832.1.
DR AlphaFoldDB; A8GDM6; -.
DR SMR; A8GDM6; -.
DR STRING; 399741.Spro_2113; -.
DR EnsemblBacteria; ABV41216; ABV41216; Spro_2113.
DR KEGG; spe:Spro_2113; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG3270; Bacteria.
DR HOGENOM; CLU_005316_6_2_6; -.
DR OrthoDB; 1064993at2; -.
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..478
FT /note="Ribosomal RNA small subunit methyltransferase F"
FT /id="PRO_0000382582"
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 478 AA; 52504 MW; 7ABC06DB8D91B69C CRC64;
MAKPACVFLP PAFLEATRAI MPADLSMDDF IAACQRPLRR SLRVNTLKIS VTDFLTLVQD
YDWRLEPIPW CAEGFWIERG DEELRLGSAA EHLSGLFYIQ EASSMLPVSA LFAGAEAPSR
VLDVAAAPGS KTTQIAALMN NQGGIVANEY SASRVKVLHA NISRCGVKNV ALTHFDGRVF
GAALPESFDA ILLDAPCSGE GVVRKDPDAM SNWSPESVTA IADTQRELID SAFHALAPGG
VMVYSTCTLN AQENQQIVNG LLATYGDAVS IEPLGDLFPG AKQALTAEGF LHVFPQIYDS
EGFFVARLRK HHSVPPLAKP SYKLGKFPFT PLSGKDSAEI AQAAAASGLA WDKTSRLWAR
DKEIWLFPAE LEALVNKIRF SRIGLKLAER FTKGYRWQHE AVIALAVADG KQRFELDATL
AQEWFHGRDL YPEPPPQTDE CIVTYQQQPL GIAKRIGSRI KNNLPRELVR DGVLDFHQ