Protein methyltransferase hemK - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0ACC1 (HEMK_ECOLI)

Last modified June 16, 2009. Version 38. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Protein methyltransferase hemK
    EC=2.1.1.-
Alternative name(s):
    Protein-glutamine N-methyltransferase hemK
    Protein-(glutamine-N(5)) MTase hemK
    M.EcoKHemKP

Gene names

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

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Methylates the translation termination release factor RF1 on 'Gln-235' and RF2 on 'Gln-252'.
Sequence similarities	Belongs to the hemK family.
Caution	Was originally (Ref.1) thought to be involved in the oxidation of protoporphyrinogen into protoporphyrin IX.
Sequence caution	The sequence BAA05915.1 differs from that shown. Reason: Frameshift at position 204.

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Ontologies

Keywords
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid methylation Inferred from electronic annotation. Source: InterPro
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protein methyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
atpG	P0ABA6	1	EBI-1122814,EBI-544306

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 277

277

Protein methyltransferase hemK

PRO_0000157156

Secondary structure

277

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0ACC1-1 [UniParc].

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

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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], CHARACTERIZATION.
[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]	"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).
[8]	"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).

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Cross-references

Sequence databases

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

AP_001837.1.
NP_415730.1.

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P0ACC1. 1 interaction.

Genome annotation databases

GeneID

945779.

GenomeReviews

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

KEGG

ecj:JW1203.
eco:b1212.

Organism-specific databases

EchoBASE

EB2323.

EcoGene

EG12424. hemK.

CMR

Search...

Phylogenomic databases

HOGENOM

P0ACC1.

OMA

P0ACC1. YVSEYTR.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12424-MON.
MetaCyc:EG12424-MON.

Family and domain databases

InterPro

IPR004556. Modification_methylase_HemK.
IPR002052. N6_adenine_Mtase_CS.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR007848. Small_mtfrase.
[Graphical view]

Pfam

PF05175. MTS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_HemK. 1 hit.

PROSITE

PS00092. N6_MTASE. 1 hit. Uncertain.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

HEMK_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:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents