Release factor glutamine methyltransferase - Escherichia coli (strain K12)

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P0ACC1 (PRMC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Release factor glutamine methyltransferase
Short name=RF MTase
EC=2.1.1.n16

Alternative name(s):
M.EcoKHemKP
N5-glutamine methyltransferase PrmC
Protein release factor methylation C
Protein-(glutamine-N5) MTase PrmC
Protein-glutamine N-methyltransferase PrmC

Gene names

Name:	prmC
Synonyms:	hemK
Ordered Locus Names:	b1212, JW1203

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3 Ref.7 Ref.9
Catalytic activity	S-adenosyl-L-methionine + glutamine in release factor = S-adenosyl-L-homocysteine + N5-methylglutamine in release factor. Ref.3 Ref.7
Subunit structure	Interacts with PrfA and PrfB. Ref.9
Disruption phenotype	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. Ref.3
Sequence similarities	Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.
Caution	Was originally thought to be involved in the oxidation of protoporphyrinogen into protoporphyrin IX (Ref.1).
Sequence caution	The sequence BAA05915.1 differs from that shown. Reason: Frameshift at position 204.

Ontologies

Keywords
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-glutamine methylation Inferred from direct assay Ref.7. Source: UniProtKB regulation of gene expression Inferred from mutant phenotype. Source: UniProtKB translational termination Inferred from mutant phenotype. Source: UniProtKB
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein-glutamine N-methyltransferase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 277

277

Release factor glutamine methyltransferase HAMAP MF_02126

PRO_0000157156

Regions

Region

117 – 121

S-adenosyl-L-methionine binding HAMAP MF_02126

Region

183 – 186

Substrate binding HAMAP MF_02126

Sites

Binding site

140

S-adenosyl-L-methionine

Binding site

168

S-adenosyl-L-methionine

Binding site

183

S-adenosyl-L-methionine

Experimental info

Mutagenesis

R → A: 17% of wild-type RF1 methylation activity. Ref.9

Mutagenesis

L → A: 60% of wild-type RF1 methylation activity. Ref.9

Mutagenesis

A → R: 7% of wild-type RF1 methylation activity. Strongly reduced affinity for S-adenosyl-L-methionine. Ref.9

Mutagenesis

F → A: 40% of wild-type RF1 methylation activity. Ref.9

Mutagenesis

E → A: 62% of wild-type RF1 methylation activity. Ref.9

Mutagenesis

E → R: 33% of wild-type RF1 methylation activity. Ref.9

Mutagenesis

183

N → A: Less than 2% of wild-type RF1 methylation activity. Ref.9

Secondary structure

277

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ACC1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 73859DF7E983B9AA
Show »

FASTA

277

30,975

        10         20         30         40         50         60 
MEYQHWLREA ISQLQASESP RRDAEILLEH VTGRGRTFIL AFGETQLTDE QCQQLDALLT 

        70         80         90        100        110        120 
RRRDGEPIAH LTGVREFWSL PLFVSPATLI PRPDTECLVE QALARLPEQP CRILDLGTGT 

       130        140        150        160        170        180 
GAIALALASE RPDCEIIAVD RMPDAVSLAQ RNAQHLAIKN IHILQSDWFS ALAGQQFAMI 

       190        200        210        220        230        240 
VSNPPYIDEQ DPHLQQGDVR FEPLTALVAA DSGMADIVHI IEQSRNALVS GGFLLLEHGW 

       250        260        270 
QQGEAVRQAF ILAGYHDVET CRDYGDNERV TLGRYYQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7883187] [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: 7543480] [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: 11805295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE. Strain: K12.
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 11847124] [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: 15223314] [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: 16364916] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

I83570.

RefSeq

NP_415730.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T43	X-ray	3.20	A	1-277	[»]
2B3T	X-ray	3.10	A	1-276	[»]

ProteinModelPortal

P0ACC1.

SMR

P0ACC1. Positions 1-276.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0ACC1. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004101; EBESCP00000004101; EBESCG00000003349.
EBESCT00000018086; EBESCP00000017377; EBESCG00000017142.

GeneID

945779.

GenomeReviews

Gene locus JW1203 in contig AP009048_GR.
Gene locus b1212 in contig U00096_GR.

KEGG

ecj:JW1203.
eco:b1212.

PATRIC

32117676. VBIEscCol129921_1260.

Organism-specific databases

EchoBASE

EB2323.

EcoGene

EG12424. prmC.

Phylogenomic databases

eggNOG

COG2890.

GeneTree

EBGT00050000009834.

HOGENOM

HBG732041.

OMA

YVSEYTR.

PhylomeDB

P0ACC1.

ProtClustDB

PRK09328.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12424-MONOMER.
MetaCyc:EG12424-MONOMER.

Gene expression databases

Genevestigator

P0ACC1.

Family and domain databases

HAMAP

MF_02126. RF_methyltr_PrmC.
[Tree]

InterPro

IPR002052. DNA_methylase_N6_adenine_CS.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR007848. Small_mtfrase.
[Graphical view]

K02493.

Pfam

PF05175. MTS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00536. HemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PRMC_ECOLI

Accession

Primary (citable) accession number: P0ACC1
Secondary accession number(s): P37186, Q46754

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents