RLMA_ECOLI
ID RLMA_ECOLI Reviewed; 269 AA.
AC P36999;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=23S rRNA (guanine(745)-N(1))-methyltransferase;
DE EC=2.1.1.187;
DE AltName: Full=23S rRNA m1G745 methyltransferase;
DE AltName: Full=Ribosomal RNA large subunit methyltransferase A;
GN Name=rlmA; Synonyms=rrmA, yebH; OrderedLocusNames=b1822, JW1811;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7984109; DOI=10.1111/j.1365-2958.1994.tb00424.x;
RA Yamanaka K., Mitani T., Ogura T., Niki H., Hiraga S.;
RT "Cloning, sequencing, and characterization of multicopy suppressors of a
RT mukB mutation in Escherichia coli.";
RL Mol. Microbiol. 13:301-312(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=9440525; DOI=10.1128/jb.180.2.359-365.1998;
RA Gustafsson C., Persson B.C.;
RT "Identification of the rrmA gene encoding the 23S rRNA m1G745
RT methyltransferase in Escherichia coli and characterization of an m1G745-
RT deficient mutant.";
RL J. Bacteriol. 180:359-365(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND ZINC IONS, AND SUBUNIT.
RX PubMed=14999102; DOI=10.1073/pnas.0400189101;
RA Das K., Acton T., Chiang Y., Shih L., Arnold E., Montelione G.T.;
RT "Crystal structure of RlmAI: implications for understanding the 23S rRNA
RT G745/G748-methylation at the macrolide antibiotic-binding site.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4041-4046(2004).
CC -!- FUNCTION: Specifically methylates the guanosine in position 745 of 23S
CC rRNA. {ECO:0000269|PubMed:9440525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(745) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(1)-methylguanosine(745) in 23S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42900, Rhea:RHEA-COMP:10273, Rhea:RHEA-COMP:10274,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.187;
CC Evidence={ECO:0000269|PubMed:9440525};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14999102}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmA family.
CC {ECO:0000305}.
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DR EMBL; D28496; BAA05855.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74892.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15633.1; -; Genomic_DNA.
DR PIR; S49049; S49049.
DR RefSeq; NP_416336.1; NC_000913.3.
DR RefSeq; WP_000010115.1; NZ_STEB01000009.1.
DR PDB; 1P91; X-ray; 2.80 A; A/B=1-269.
DR PDBsum; 1P91; -.
DR AlphaFoldDB; P36999; -.
DR SMR; P36999; -.
DR BioGRID; 4260324; 21.
DR IntAct; P36999; 18.
DR STRING; 511145.b1822; -.
DR jPOST; P36999; -.
DR PaxDb; P36999; -.
DR PRIDE; P36999; -.
DR DNASU; 946340; -.
DR EnsemblBacteria; AAC74892; AAC74892; b1822.
DR EnsemblBacteria; BAA15633; BAA15633; BAA15633.
DR GeneID; 946340; -.
DR KEGG; ecj:JW1811; -.
DR KEGG; eco:b1822; -.
DR PATRIC; fig|1411691.4.peg.429; -.
DR EchoBASE; EB2122; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_050931_0_0_6; -.
DR InParanoid; P36999; -.
DR OMA; MTPHGWR; -.
DR PhylomeDB; P36999; -.
DR BioCyc; EcoCyc:EG12207-MON; -.
DR BioCyc; MetaCyc:EG12207-MON; -.
DR BRENDA; 2.1.1.187; 2026.
DR EvolutionaryTrace; P36999; -.
DR PRO; PR:P36999; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0052911; F:23S rRNA (guanine(745)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008989; F:rRNA (guanine-N1-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR PIRSF; PIRSF018249; MyrA_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..269
FT /note="23S rRNA (guanine(745)-N(1))-methyltransferase"
FT /id="PRO_0000097444"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14999102,
FT ECO:0007744|PDB:1P91"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14999102,
FT ECO:0007744|PDB:1P91"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14999102,
FT ECO:0007744|PDB:1P91"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:14999102,
FT ECO:0007744|PDB:1P91"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:14999102"
FT BINDING 96..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:14999102"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:14999102"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:1P91"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:1P91"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1P91"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 208..223
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1P91"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1P91"
FT STRAND 252..267
FT /evidence="ECO:0007829|PDB:1P91"
SQ SEQUENCE 269 AA; 30419 MW; F4A154A6EC3FB6D6 CRC64;
MSFSCPLCHQ PLSREKNSYI CPQRHQFDMA KEGYVNLLPV QHKRSRDPGD SAEMMQARRA
FLDAGHYQPL RDAIVAQLRE RLDDKATAVL DIGCGEGYYT HAFADALPEI TTFGLDVSKV
AIKAAAKRYP QVTFCVASSH RLPFSDTSMD AIIRIYAPCK AEELARVVKP GGWVITATPG
PRHLMELKGL IYNEVHLHAP HAEQLEGFTL QQSAELCYPM RLRGDEAVAL LQMTPFAWRA
KPEVWQTLAA KEVFDCQTDF NIHLWQRSY
