CFR_CLOBL
ID CFR_CLOBL Reviewed; 344 AA.
AC A7GH77;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase Cfr {ECO:0000255|HAMAP-Rule:MF_01873};
DE EC=2.1.1.224 {ECO:0000255|HAMAP-Rule:MF_01873};
DE AltName: Full=23S rRNA (adenine(2503)-C(8))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01873};
DE AltName: Full=23S rRNA m8A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01873};
GN Name=cfr {ECO:0000255|HAMAP-Rule:MF_01873}; OrderedLocusNames=CLI_2911;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S
CC rRNA. Confers resistance to some classes of antibiotics.
CC {ECO:0000255|HAMAP-Rule:MF_01873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin]
CC + 2 S-adenosyl-L-methionine = 5'-deoxyadenosine + 8-
CC methyladenosine(2503) in 23S rRNA + L-methionine + 2 oxidized [2Fe-
CC 2S]-[ferredoxin] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42632,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152,
CC Rhea:RHEA-COMP:10153, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74543;
CC EC=2.1.1.224; Evidence={ECO:0000255|HAMAP-Rule:MF_01873};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01873};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_01873};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01873}.
CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving
CC intermediate methylation of a conserved cysteine residue.
CC {ECO:0000255|HAMAP-Rule:MF_01873}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. Cfr
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01873}.
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DR EMBL; CP000728; ABS41349.1; -; Genomic_DNA.
DR RefSeq; WP_012100648.1; NC_009699.1.
DR AlphaFoldDB; A7GH77; -.
DR SMR; A7GH77; -.
DR EnsemblBacteria; ABS41349; ABS41349; CLI_2911.
DR KEGG; cbf:CLI_2911; -.
DR HOGENOM; CLU_029101_0_2_9; -.
DR OMA; RIFFEWT; -.
DR Proteomes; UP000002410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01873; 23SrRNA_methyltr_Cfr; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040072; Methyltransferase_A.
DR InterPro; IPR022881; rRNA_lsu_MeTfrase_Cfr.
DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30544; PTHR30544; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF006004; CHP00048; 1.
DR SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
DR SFLD; SFLDF00296; adenosine_C8_methyltransferase; 1.
DR TIGRFAMs; TIGR04432; rSAM_Cfr; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Antibiotic resistance; Cytoplasm; Disulfide bond; Iron;
KW Iron-sulfur; Metal-binding; Methyltransferase; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..344
FT /note="Ribosomal RNA large subunit methyltransferase Cfr"
FT /id="PRO_0000350119"
FT DOMAIN 97..330
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT ACT_SITE 335
FT /note="S-methylcysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 157..158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 211..213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 292
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT DISULFID 104..335
FT /note="(transient)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
SQ SEQUENCE 344 AA; 39067 MW; ED9C1308F4E333A9 CRC64;
MKQTKTKYGK MKQIVSNLKL PDYRYEQLTK AIFHQRIDNF DDMHILPKVL RMSLVNEFGK
NVSSVIPVFS QDSKQAQKLL FELTDGERIE AVGLKYKQGW ESFCISSQCG CGFGCRFCAT
GSAGFKRNLT ADEITDQLLY FYFNDHRLNS ISFMGMGEAF ANPELFDAVK ILTDQNLFGL
SQRRITISTI GIIPGIQSLT QKFPQVNLAF SLHSPFESQR SDLMPINKRF PLNQVMKTLD
EHIIHTGRRV FIAYIMLEGI NDSKEHAEAV VGLLKNRGSW EHLYHIDLIP YNSTDKTTFK
FQSSNAIKQF CSTLKKAGIS ATVRTQFGSE ISAACGQLCY ENEL
