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CFR_STAWA
ID   CFR_STAWA               Reviewed;         349 AA.
AC   A2AXI2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
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};
OS   Staphylococcus warneri.
OG   Plasmid pSCFS6.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=11562A;
RX   PubMed=17145796; DOI=10.1128/aac.01340-06;
RA   Kehrenberg C., Aarestrup F.M., Schwarz S.;
RT   "IS21-558 insertion sequences are involved in the mobility of the
RT   multiresistance gene cfr.";
RL   Antimicrob. Agents Chemother. 51:483-487(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; AM408573; CAL64019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2AXI2; -.
DR   SMR; A2AXI2; -.
DR   KEGG; ag:CAL64019; -.
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; 2.
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; Plasmid; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..349
FT                   /note="Ribosomal RNA large subunit methyltransferase Cfr"
FT                   /id="PRO_0000350446"
FT   DOMAIN          98..333
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT   ACT_SITE        338
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT   BINDING         112
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         116
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         119
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         158..159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT   BINDING         189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT   BINDING         212..214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
FT   DISULFID        105..338
FT                   /note="(transient)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01873"
SQ   SEQUENCE   349 AA;  39862 MW;  53C5F48D61BE94CD CRC64;
     MNFNNKTKYG KIQEFLRSNN EPDYRIKQIT NAIFKQRISR FEDMKVLPKL LREDLINNFG
     ETVLNIKLLA EQNSEQVTKV LFEVSKNERV ETVNMKYKAG WESFCISSQC GCNFGCKFCA
     TGDIGLKKNL TVDEITDQVL YFHLLGHQID SISFMGMGEA LANRQVFDAL DSFTDPNLFA
     LSPRRLSIST IGIIPSIKKI TQEYPQVNLT FSLHSPYSEE RSKLMPINDR YPIDEVMNIL
     DEHIRLTSRK VYIAYIMLPG VNDSLEHANE VVSLLKSRYK SGKLYHVNLI RYNPTISAPE
     MYGEANEGQV EAFYKVLKSA GIHVTIRSQF GIDIDAACGQ LYGNYQNSQ
 
 
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