PRMB_ECOLI
ID PRMB_ECOLI Reviewed; 310 AA.
AC P39199; P76939; P78252;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=50S ribosomal protein L3 glutamine methyltransferase;
DE Short=L3 MTase;
DE EC=2.1.1.298;
DE AltName: Full=N5-glutamine methyltransferase PrmB;
GN Name=prmB; Synonyms=yfcB; OrderedLocusNames=b2330, JW5841;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 172-310.
RX PubMed=2182772; DOI=10.1099/00221287-136-2-353;
RA Charles I.G., Lamb H.K., Pickard D., Dougan G., Hawkins A.R.;
RT "Isolation, characterization and nucleotide sequences of the aroC genes
RT encoding chorismate synthase from Salmonella typhi and Escherichia coli.";
RL J. Gen. Microbiol. 136:353-358(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 159-310.
RC STRAIN=K12;
RX PubMed=2969724; DOI=10.1042/bj2510313;
RA White P.J., Millar G., Coggins J.R.;
RT "The overexpression, purification and complete amino acid sequence of
RT chorismate synthase from Escherichia coli K12 and its comparison with the
RT enzyme from Neurospora crassa.";
RL Biochem. J. 251:313-322(1988).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND GENE NAME.
RC STRAIN=K12;
RX PubMed=11847124; DOI=10.1093/emboj/21.4.769;
RA Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.;
RT "The hemK gene in Escherichia coli encodes the N(5)-glutamine
RT methyltransferase that modifies peptide release factors.";
RL EMBO J. 21:769-778(2002).
CC -!- FUNCTION: Specifically methylates the 50S ribosomal protein L3 on 'Gln-
CC 150'. Does not methylate the translation termination release factors
CC RF1 and RF2. {ECO:0000269|PubMed:11847124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[ribosomal protein uL3] + S-adenosyl-L-methionine
CC = H(+) + N(5)-methyl-L-glutaminyl-[ribosomal protein uL3] + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:45020, Rhea:RHEA-COMP:11063,
CC Rhea:RHEA-COMP:11064, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC EC=2.1.1.298; Evidence={ECO:0000269|PubMed:11847124};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M33021; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC75390.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16188.2; -; Genomic_DNA.
DR EMBL; M27714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y00720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M33021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H65005; H65005.
DR RefSeq; NP_416833.4; NC_000913.3.
DR RefSeq; WP_001300582.1; NZ_LN832404.1.
DR AlphaFoldDB; P39199; -.
DR SMR; P39199; -.
DR BioGRID; 4261060; 26.
DR DIP; DIP-11976N; -.
DR IntAct; P39199; 8.
DR STRING; 511145.b2330; -.
DR jPOST; P39199; -.
DR PaxDb; P39199; -.
DR PRIDE; P39199; -.
DR EnsemblBacteria; AAC75390; AAC75390; b2330.
DR EnsemblBacteria; BAA16188; BAA16188; BAA16188.
DR GeneID; 946805; -.
DR KEGG; ecj:JW5841; -.
DR KEGG; eco:b2330; -.
DR PATRIC; fig|511145.12.peg.2426; -.
DR EchoBASE; EB2343; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_5_1_6; -.
DR InParanoid; P39199; -.
DR OMA; IYYGHGT; -.
DR PhylomeDB; P39199; -.
DR BioCyc; EcoCyc:EG12449-MON; -.
DR BioCyc; MetaCyc:EG12449-MON; -.
DR BRENDA; 2.1.1.298; 2026.
DR PRO; PR:P39199; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IMP:EcoCyc.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_02125; L3_methyltr_PrmB; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR017127; Ribosome_L3_Gln-N5_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037167; Mtase_YfcB_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03533; L3_gln_methyl; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..310
FT /note="50S ribosomal protein L3 glutamine
FT methyltransferase"
FT /id="PRO_0000088003"
SQ SEQUENCE 310 AA; 35002 MW; 3EE8F2D45AFC3760 CRC64;
MDKIFVDEAV NELQTIQDML RWSVSRFSAA NIWYGHGTDN PWDEAVQLVL PSLYLPLDIP
EDMRTARLTS SEKHRIVERV IRRVNERIPV AYLTNKAWFC GHEFYVDERV LVPRSPIGEL
INNKFAGLIS KQPQHILDMC TGSGCIAIAC AYAFPDAEVD AVDISPDALA VAEQNIEEHG
LIHNVIPIRS DLFRDLPKVQ YDLIVTNPPY VDAEDMSDLP NEYRHEPELG LASGTDGLKL
TRRILGNAAD YLADDGVLIC EVGNSMVHLM EQYPDVPFTW LEFDNGGDGV FMLTKEQLIA
AREHFAIYKD
