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   02-SEP-2026, entry version 138.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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 = N(5)-methyl-L-glutaminyl-[peptide chain release factor]
CC         + S-adenosyl-L-homocysteine + H(+); 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_CP009789.1.
DR   PDB; 1T43; X-ray; 3.20 A; A=1-277.
DR   PDB; 2B3T; X-ray; 3.10 A; A=1-276.
DR   AlphaFoldDB; P0ACC1; -.
DR   SMR; P0ACC1; -.
DR   BioGRID; 4260113; 37.
DR   FunCoup; P0ACC1; 645.
DR   IntAct; P0ACC1; 1.
DR   STRING; 511145.b1212; -.
DR   DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR   PaxDb; 511145-b1212; -.
DR   EnsemblBacteria; AAC74296; AAC74296; b1212.
DR   GeneID; 75171323; -.
DR   GeneID; 945779; -.
DR   KEGG; ecj:JW1203; -.
DR   KEGG; eco:b1212; -.
DR   KEGG; ecoc:C3026_07120; -.
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; DFDARYW; -.
DR   OrthoDB; 9800643at2; -.
DR   PhylomeDB; P0ACC1; -.
DR   BioCyc; EcoCyc:EG12424-MONOMER; -.
DR   BioCyc; MetaCyc:EG12424-MONOMER; -.
DR   BRENDA; 2.1.1.297; 2026.
DR   EvolutionaryTrace; P0ACC1; -.
DR   PRO; PR:P0ACC1; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0ACC1; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0102559; F:peptide chain release factor N(5)-glutamine methyltransferase activity; EXP:UniProtKB.
DR   GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
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; IMP:EcoCyc.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0006415; P:translational termination; IMP:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   FunFam; 1.10.8.10:FF:000032; Release factor glutamine methyltransferase; 1.
DR   FunFam; 3.40.50.150:FF:000053; Release factor glutamine methyltransferase; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR050320; N5-glutamine_MTase.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; RF_methyltr_PrmC.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   NCBIfam; TIGR00536; hemK_fam; 1.
DR   NCBIfam; TIGR03534; RF_mod_PrmC; 1.
DR   PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PDBsum; 1T43; -.
DR   PDBsum; 2B3T; -.
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
//