CFR_BACVZ
ID CFR_BACVZ Reviewed; 349 AA.
AC A7Z1T2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=RBAM_005660;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS72958.1; -; Genomic_DNA.
DR RefSeq; WP_012116915.1; NC_009725.2.
DR AlphaFoldDB; A7Z1T2; -.
DR SMR; A7Z1T2; -.
DR STRING; 326423.RBAM_005660; -.
DR EnsemblBacteria; ABS72958; ABS72958; RBAM_005660.
DR KEGG; bay:RBAM_005660; -.
DR HOGENOM; CLU_029101_0_2_9; -.
DR OMA; RIFFEWT; -.
DR Proteomes; UP000001120; 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 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; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..349
FT /note="Ribosomal RNA large subunit methyltransferase Cfr"
FT /id="PRO_0000350025"
FT DOMAIN 96..331
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT ACT_SITE 336
FT /note="S-methylcysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 110
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 114
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 117
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 156..157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 210..212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT DISULFID 103..336
FT /note="(transient)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
SQ SEQUENCE 349 AA; 40078 MW; 69E507B269C9F0DB CRC64;
MQQKNKYIRI QEFLKQNKFP DFRMNQIKNA VFQGRINHFN EITVLPKSLR KLLIEEFGES
ILNIAPLKVQ HSEQVTKVLF EISGDEKIET VNMKYKAGWE SFCISSQCGC HFGCKFCATG
DIGLKRNLTS DEMTDQILYF HLKGHSIDSI SFMGMGEALA NVQVFDALHV LTNPELFALS
PRRLSISTIG IIPGIKKITQ DYPQVNLTFS LHSPFNEQRS KLMPINERYP LLEVMDTLDE
HIRVTSRKVY IAYIMLPGVN DSIDHANEVV NLLRSRYKRG NLFHVNIIRY NPTVSSPMRF
EEVNEKQVVN FYKKLKSAGI NVTVRSQFGI DIDAACGQLY GNYQKNKNQ
