(data stored in SCRATCH3701 zone)

SWISSPROT: RLMC_ECOBW

ID   RLMC_ECOBW              Reviewed;         375 AA.
AC   C4ZY31;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 57.
DE   RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000255|HAMAP-Rule:MF_01012};
DE            EC=2.1.1.189 {ECO:0000255|HAMAP-Rule:MF_01012};
DE   AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01012};
GN   Name=rlmC {ECO:0000255|HAMAP-Rule:MF_01012}; Synonyms=rumB;
GN   OrderedLocusNames=BWG_0712;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747
CC       (m5U747) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC         methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01012};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01012}.
DR   EMBL; CP001396; ACR61752.1; -; Genomic_DNA.
DR   RefSeq; WP_001149682.1; NC_012759.1.
DR   SMR; C4ZY31; -.
DR   EnsemblBacteria; ACR61752; ACR61752; BWG_0712.
DR   KEGG; ebw:BWG_0712; -.
DR   HOGENOM; HOG000218547; -.
DR   KO; K03212; -.
DR   OMA; SCQWLEK; -.
DR   BioCyc; ECOL595496:BWG_RS03995-MONOMER; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01012; 23SrRNA_methyltr_RlmC; 1.
DR   InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02085; meth_trns_rumB; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4ZY31.
DR   SWISS-2DPAGE; C4ZY31.
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..375
FT                   /note="23S rRNA (uracil(747)-C(5))-methyltransferase RlmC"
FT                   /id="PRO_1000213201"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           3
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           11
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           14
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   METAL           87
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         212
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         241
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         262
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
FT   BINDING         307
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01012"
SQ   SEQUENCE   375 AA;  41956 MW;  EDFE591BE2B9DE7D CRC64;
     MQCALYDAGR CRSCQWIMQP IPEQLSAKTA DLKNLLADFP VEEWCAPVSG PEQGFRNKAK
     MVVSGSVEKP LLGMLHRDGT PEDLCDCPLY PASFAPVFAA LKPFIARAGL TPYNVARKRG
     ELKYILLTES QSDGGMMLRF VLRSDTKLAQ LRKALPWLHE QLPQLKVITV NIQPVHMAIM
     EGETEIYLTE QQALAERFND VPLWIRPQSF FQTNPAVASQ LYATARDWVR QLPVKHMWDL
     FCGVGGFGLH CATPDMQLTG IEIASEAIAC AKQSAAELGL TRLQFQALDS TQFATAQGDV
     PELVLVNPPR RGIGKPLCDY LSTMAPRFII YSSCNAQTMA KDIRELPGFR IERVQLFDMF
     PHTAHYEVLT LLVKQ
//

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