PRMC_ECOLI
ID PRMC_ECOLI Reviewed; 277 AA.
AC P0ACC1; P37186; Q46754;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126};
DE Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126};
DE EC=2.1.1.297 {ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124};
DE AltName: Full=M.EcoKHemKP;
DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein release factor methylation C;
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126};
GN Name=prmC; Synonyms=hemK; OrderedLocusNames=b1212, JW1203;
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=7883187; DOI=10.1016/0378-1119(94)00805-3;
RA Nakayashiki T., Nishimura K., Inokuchi H.;
RT "Cloning and sequencing of a previously unidentified gene that is involved
RT in the biosynthesis of heme in Escherichia coli.";
RL Gene 153:67-70(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7543480; DOI=10.1128/jb.177.15.4488-4500.1995;
RA Strohmaier H., Remler P., Renner W., Hoegenauer G.;
RT "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic
RT acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is
RT growth phase regulated primarily at the transcriptional level in
RT Escherichia coli K-12.";
RL J. Bacteriol. 177:4488-4500(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11805295; DOI=10.1073/pnas.032488499;
RA Nakahigashi K., Kubo N., Narita S., Shimaoka T., Goto S., Oshima T.,
RA Mori H., Maeda M., Wada C., Inokuchi H.;
RT "HemK, a class of protein methyl transferase with similarity to DNA methyl
RT transferases, methylates polypeptide chain release factors, and hemK
RT knockout induces defects in translational termination.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1473-1478(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
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 [6]
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 [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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RX PubMed=15223314; DOI=10.1016/j.jmb.2004.05.019;
RA Yang Z., Shipman L., Zhang M., Anton B.P., Roberts R.J., Cheng X.;
RT "Structural characterization and comparative phylogenetic analysis of
RT Escherichia coli HemK, a protein (N5)-glutamine methyltransferase.";
RL J. Mol. Biol. 340:695-706(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH RELEASE FACTOR RF1
RP AND S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, MUTAGENESIS OF ARG-36; LEU-40;
RP ALA-41; PHE-42; GLU-44 AND ASN-183, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=16364916; DOI=10.1016/j.molcel.2005.10.025;
RA Graille M., Heurgue-Hamard V., Champ S., Mora L., Scrima N., Ulryck N.,
RA van Tilbeurgh H., Buckingham R.H.;
RT "Molecular basis for bacterial class I release factor methylation by
RT PrmC.";
RL Mol. Cell 20:917-927(2005).
CC -!- FUNCTION: Methylates the class 1 translation termination release
CC factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-
CC 252' in RF2. {ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124,
CC ECO:0000269|PubMed:16364916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000269|PubMed:11805295, ECO:0000269|PubMed:11847124};
CC -!- SUBUNIT: Interacts with PrfA and PrfB. {ECO:0000269|PubMed:15223314,
CC ECO:0000269|PubMed:16364916}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene suffer severe growth
CC defects, but also show a global shift in gene expression to anaerobic
CC respiration. Also shows defects in translational termination via an
CC enhanced rate of read-through of nonsense codons and induction of
CC transfer-mRNA-mediated tagging of proteins within the cell.
CC {ECO:0000269|PubMed:11805295}.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily. {ECO:0000255|HAMAP-Rule:MF_02126}.
CC -!- CAUTION: Was originally thought to be involved in the oxidation of
CC protoporphyrinogen into protoporphyrin IX.
CC {ECO:0000305|PubMed:7883187}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05915.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D28567; BAA05915.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18555; AAC43438.1; -; Genomic_DNA.
DR EMBL; AB078778; BAB84109.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74296.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36070.1; -; Genomic_DNA.
DR PIR; I83570; I83570.
DR RefSeq; NP_415730.1; NC_000913.3.
DR RefSeq; WP_000456467.1; NZ_SSZK01000010.1.
DR PDB; 1T43; X-ray; 3.20 A; A=1-277.
DR PDB; 2B3T; X-ray; 3.10 A; A=1-276.
DR PDBsum; 1T43; -.
DR PDBsum; 2B3T; -.
DR AlphaFoldDB; P0ACC1; -.
DR SMR; P0ACC1; -.
DR BioGRID; 4260113; 35.
DR IntAct; P0ACC1; 1.
DR STRING; 511145.b1212; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR PaxDb; P0ACC1; -.
DR PRIDE; P0ACC1; -.
DR EnsemblBacteria; AAC74296; AAC74296; b1212.
DR EnsemblBacteria; BAA36070; BAA36070; BAA36070.
DR GeneID; 58389078; -.
DR GeneID; 945779; -.
DR KEGG; ecj:JW1203; -.
DR KEGG; eco:b1212; -.
DR PATRIC; fig|1411691.4.peg.1072; -.
DR EchoBASE; EB2323; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_3_1_6; -.
DR InParanoid; P0ACC1; -.
DR OMA; FDARYWE; -.
DR PhylomeDB; P0ACC1; -.
DR BioCyc; EcoCyc:EG12424-MON; -.
DR BioCyc; MetaCyc:EG12424-MON; -.
DR BRENDA; 2.1.1.297; 2026.
DR EvolutionaryTrace; P0ACC1; -.
DR PRO; PR:P0ACC1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006415; P:translational termination; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..277
FT /note="Release factor glutamine methyltransferase"
FT /id="PRO_0000157156"
FT BINDING 117..121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02126,
FT ECO:0000305|PubMed:15223314"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:15223314,
FT ECO:0000305|PubMed:16364916"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:15223314,
FT ECO:0000305|PubMed:16364916"
FT BINDING 183..186
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16364916"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:15223314"
FT MUTAGEN 36
FT /note="R->A: 17% of wild-type RF1 methylation activity."
FT /evidence="ECO:0000269|PubMed:16364916"
FT MUTAGEN 40
FT /note="L->A: 60% of wild-type RF1 methylation activity."
FT /evidence="ECO:0000269|PubMed:16364916"
FT MUTAGEN 41
FT /note="A->R: 7% of wild-type RF1 methylation activity.
FT Strongly reduced affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:16364916"
FT MUTAGEN 42
FT /note="F->A: 40% of wild-type RF1 methylation activity."
FT /evidence="ECO:0000269|PubMed:16364916"
FT MUTAGEN 44
FT /note="E->A: 62% of wild-type RF1 methylation activity."
FT /evidence="ECO:0000269|PubMed:16364916"
FT MUTAGEN 44
FT /note="E->R: 33% of wild-type RF1 methylation activity."
FT /evidence="ECO:0000269|PubMed:16364916"
FT MUTAGEN 183
FT /note="N->A: Less than 2% of wild-type RF1 methylation
FT activity."
FT /evidence="ECO:0000269|PubMed:16364916"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2B3T"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2B3T"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1T43"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2B3T"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:2B3T"
SQ SEQUENCE 277 AA; 30975 MW; 73859DF7E983B9AA CRC64;
MEYQHWLREA ISQLQASESP RRDAEILLEH VTGRGRTFIL AFGETQLTDE QCQQLDALLT
RRRDGEPIAH LTGVREFWSL PLFVSPATLI PRPDTECLVE QALARLPEQP CRILDLGTGT
GAIALALASE RPDCEIIAVD RMPDAVSLAQ RNAQHLAIKN IHILQSDWFS ALAGQQFAMI
VSNPPYIDEQ DPHLQQGDVR FEPLTALVAA DSGMADIVHI IEQSRNALVS GGFLLLEHGW
QQGEAVRQAF ILAGYHDVET CRDYGDNERV TLGRYYQ
