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Protein

Release factor glutamine methyltransferase

Gene

prmC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401S-adenosyl-L-methionine2 Publications
Binding sitei168 – 1681S-adenosyl-L-methionine2 Publications
Binding sitei183 – 1831S-adenosyl-L-methionine1 Publication

GO - Molecular functioni

  • nucleic acid binding Source: InterPro
  • protein-glutamine N-methyltransferase activity Source: UniProtKB
  • protein methyltransferase activity Source: UniProtKB
  • S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB

GO - Biological processi

  • peptidyl-glutamine methylation Source: UniProtKB
  • protein methylation Source: UniProtKB
  • regulation of gene expression Source: UniProtKB
  • translational termination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:EG12424-MONOMER.
ECOL316407:JW1203-MONOMER.
MetaCyc:EG12424-MONOMER.
BRENDAi2.1.1.297. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Release factor glutamine methyltransferaseUniRule annotation (EC:2.1.1.2972 Publications)
Short name:
RF MTaseUniRule annotation
Alternative name(s):
M.EcoKHemKP
N5-glutamine methyltransferase PrmCUniRule annotation
Protein release factor methylation C
Protein-(glutamine-N5) MTase PrmCUniRule annotation
Protein-glutamine N-methyltransferase PrmCUniRule annotation
Gene namesi
Name:prmC
Synonyms:hemK
Ordered Locus Names:b1212, JW1203
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12424. prmC.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene suffer severe growth defects, but also show a global shift in gene expression to anaerobic respiration. Also show defects in translational termination via an enhanced rate of read-through of nonsense codons and induction of transfer-mRNA-mediated tagging of proteins within the cell.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361R → A: 17% of wild-type RF1 methylation activity. 1 Publication
Mutagenesisi40 – 401L → A: 60% of wild-type RF1 methylation activity. 1 Publication
Mutagenesisi41 – 411A → R: 7% of wild-type RF1 methylation activity. Strongly reduced affinity for S-adenosyl-L-methionine. 1 Publication
Mutagenesisi42 – 421F → A: 40% of wild-type RF1 methylation activity. 1 Publication
Mutagenesisi44 – 441E → A: 62% of wild-type RF1 methylation activity. 1 Publication
Mutagenesisi44 – 441E → R: 33% of wild-type RF1 methylation activity. 1 Publication
Mutagenesisi183 – 1831N → A: Less than 2% of wild-type RF1 methylation activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Release factor glutamine methyltransferasePRO_0000157156Add
BLAST

Proteomic databases

PaxDbiP0ACC1.

Interactioni

Subunit structurei

Interacts with PrfA and PrfB.2 Publications

Protein-protein interaction databases

IntActiP0ACC1. 1 interaction.
STRINGi511145.b1212.

Structurei

Secondary structure

1
277
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Turni13 – 164Combined sources
Helixi20 – 3213Combined sources
Helixi36 – 416Combined sources
Turni42 – 443Combined sources
Helixi49 – 6315Combined sources
Helixi68 – 714Combined sources
Beta strandi74 – 774Combined sources
Beta strandi80 – 834Combined sources
Helixi95 – 10511Combined sources
Beta strandi112 – 1165Combined sources
Helixi122 – 1309Combined sources
Beta strandi134 – 1396Combined sources
Helixi143 – 15614Combined sources
Beta strandi160 – 1645Combined sources
Helixi170 – 1723Combined sources
Beta strandi177 – 1826Combined sources
Helixi192 – 1954Combined sources
Helixi198 – 2003Combined sources
Turni205 – 2073Combined sources
Helixi210 – 2134Combined sources
Helixi215 – 22410Combined sources
Helixi225 – 2273Combined sources
Beta strandi228 – 23710Combined sources
Helixi240 – 2423Combined sources
Helixi243 – 25210Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi266 – 2749Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T43X-ray3.20A1-277[»]
2B3TX-ray3.10A1-276[»]
ProteinModelPortaliP0ACC1.
SMRiP0ACC1. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACC1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 1215S-adenosyl-L-methionine bindingUniRule annotation1 Publication
Regioni183 – 1864Substrate binding1 Publication

Sequence similaritiesi

Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EQY. Bacteria.
COG2890. LUCA.
HOGENOMiHOG000076274.
InParanoidiP0ACC1.
KOiK02493.
OMAiHGWTQGE.
OrthoDBiEOG68Q0SZ.
PhylomeDBiP0ACC1.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_02126. RF_methyltr_PrmC.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR025714. Methyltranfer_dom.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.

Sequencei

Sequence statusi: Complete.

P0ACC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYQHWLREA ISQLQASESP RRDAEILLEH VTGRGRTFIL AFGETQLTDE
60 70 80 90 100
QCQQLDALLT RRRDGEPIAH LTGVREFWSL PLFVSPATLI PRPDTECLVE
110 120 130 140 150
QALARLPEQP CRILDLGTGT GAIALALASE RPDCEIIAVD RMPDAVSLAQ
160 170 180 190 200
RNAQHLAIKN IHILQSDWFS ALAGQQFAMI VSNPPYIDEQ DPHLQQGDVR
210 220 230 240 250
FEPLTALVAA DSGMADIVHI IEQSRNALVS GGFLLLEHGW QQGEAVRQAF
260 270
ILAGYHDVET CRDYGDNERV TLGRYYQ
Length:277
Mass (Da):30,975
Last modified:November 8, 2005 - v1
Checksum:i73859DF7E983B9AA
GO

Sequence cautioni

The sequence BAA05915.1 differs from that shown. Reason: Frameshift at position 204. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28567 Genomic DNA. Translation: BAA05915.1. Frameshift.
U18555 Genomic DNA. Translation: AAC43438.1.
AB078778 Genomic DNA. Translation: BAB84109.1.
U00096 Genomic DNA. Translation: AAC74296.1.
AP009048 Genomic DNA. Translation: BAA36070.1.
PIRiI83570.
RefSeqiNP_415730.1. NC_000913.3.
WP_000456467.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74296; AAC74296; b1212.
BAA36070; BAA36070; BAA36070.
GeneIDi945779.
KEGGiecj:JW1203.
eco:b1212.
PATRICi32117676. VBIEscCol129921_1260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28567 Genomic DNA. Translation: BAA05915.1. Frameshift.
U18555 Genomic DNA. Translation: AAC43438.1.
AB078778 Genomic DNA. Translation: BAB84109.1.
U00096 Genomic DNA. Translation: AAC74296.1.
AP009048 Genomic DNA. Translation: BAA36070.1.
PIRiI83570.
RefSeqiNP_415730.1. NC_000913.3.
WP_000456467.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T43X-ray3.20A1-277[»]
2B3TX-ray3.10A1-276[»]
ProteinModelPortaliP0ACC1.
SMRiP0ACC1. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0ACC1. 1 interaction.
STRINGi511145.b1212.

Proteomic databases

PaxDbiP0ACC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74296; AAC74296; b1212.
BAA36070; BAA36070; BAA36070.
GeneIDi945779.
KEGGiecj:JW1203.
eco:b1212.
PATRICi32117676. VBIEscCol129921_1260.

Organism-specific databases

EchoBASEiEB2323.
EcoGeneiEG12424. prmC.

Phylogenomic databases

eggNOGiENOG4105EQY. Bacteria.
COG2890. LUCA.
HOGENOMiHOG000076274.
InParanoidiP0ACC1.
KOiK02493.
OMAiHGWTQGE.
OrthoDBiEOG68Q0SZ.
PhylomeDBiP0ACC1.

Enzyme and pathway databases

BioCyciEcoCyc:EG12424-MONOMER.
ECOL316407:JW1203-MONOMER.
MetaCyc:EG12424-MONOMER.
BRENDAi2.1.1.297. 2026.

Miscellaneous databases

EvolutionaryTraceiP0ACC1.
PROiP0ACC1.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_02126. RF_methyltr_PrmC.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR025714. Methyltranfer_dom.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli."
    Nakayashiki T., Nishimura K., Inokuchi H.
    Gene 153:67-70(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
    Strohmaier H., Remler P., Renner W., Hoegenauer G.
    J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination."
    Nakahigashi K., Kubo N., Narita S., Shimaoka T., Goto S., Oshima T., Mori H., Maeda M., Wada C., Inokuchi H.
    Proc. Natl. Acad. Sci. U.S.A. 99:1473-1478(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors."
    Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.
    EMBO J. 21:769-778(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, GENE NAME.
    Strain: K12.
  8. "Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase."
    Yang Z., Shipman L., Zhang M., Anton B.P., Roberts R.J., Cheng X.
    J. Mol. Biol. 340:695-706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
  9. "Molecular basis for bacterial class I release factor methylation by PrmC."
    Graille M., Heurgue-Hamard V., Champ S., Mora L., Scrima N., Ulryck N., van Tilbeurgh H., Buckingham R.H.
    Mol. Cell 20:917-927(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH RELEASE FACTOR RF1 AND S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, MUTAGENESIS OF ARG-36; LEU-40; ALA-41; PHE-42; GLU-44 AND ASN-183, SUBUNIT.
    Strain: K12.

Entry informationi

Entry nameiPRMC_ECOLI
AccessioniPrimary (citable) accession number: P0ACC1
Secondary accession number(s): P37186, Q46754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: January 20, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be involved in the oxidation of protoporphyrinogen into protoporphyrin IX.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.