CFR_CLOBH
ID CFR_CLOBH Reviewed; 344 AA.
AC A5I5U3; A7G704;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
GN OrderedLocusNames=CBO2857, CLC_2734;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000727; ABS37379.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL84423.1; -; Genomic_DNA.
DR RefSeq; WP_011987126.1; NC_009698.1.
DR RefSeq; YP_001255356.1; NC_009495.1.
DR RefSeq; YP_001388569.1; NC_009698.1.
DR AlphaFoldDB; A5I5U3; -.
DR SMR; A5I5U3; -.
DR PRIDE; A5I5U3; -.
DR GeneID; 5184333; -.
DR KEGG; cbh:CLC_2734; -.
DR KEGG; cbo:CBO2857; -.
DR PATRIC; fig|413999.7.peg.2841; -.
DR HOGENOM; CLU_029101_0_2_9; -.
DR OMA; RIFFEWT; -.
DR PRO; PR:A5I5U3; -.
DR Proteomes; UP000001986; 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; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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 SFLD; SFLDS00029; Radical_SAM; 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; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..344
FT /note="Ribosomal RNA large subunit methyltransferase Cfr"
FT /id="PRO_0000350117"
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; 39161 MW; F60B1D4966C7B27E CRC64;
MKQTKTKYGK MKQIASNLKL PDYRYEQLTK AIFHQRIDNF HDMHILPKAL RIALVNEFGK
NVSSVTPIFS QDSKQAQKLL FELTDGERIE AVGLKYKQGW ESFCISSQCG CSFGCRFCAT
GSAGFKRNLT ADEITDQLLY FYFNDHRLNS ISFMGMGEAF ANPELFDAVK ILTDQNLFGL
SQRRITISTI GIIPGIQRLT KEFPQVNLAF SLHSPFESQR SDLMPINKRF PLNEVMKTLD
EHIIHTGRRV FIAYIMLEGI NDSKEHAEAI IGLLRNRGSW EHLYHIDLIP YNSTDKTTFK
FQSSSAIKQF CSTLKKASIS ATVRTQFGSE ISAACGQLCY ENEL
