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P08957 (T1MK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type I restriction enzyme EcoKI M protein
Short name=M.EcoKI
EC=2.1.1.72
Gene names
Name:hsdM
Synonyms:hsm
Ordered Locus Names:b4349, JW4312
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoKI enzyme recognizes 5'-AACN6GTGC-3'.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Subunit structure

The type I restriction/modification system is composed of three polypeptides R, M and S.

Miscellaneous

Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

Sequence similarities

Belongs to the N(4)/N(6)-methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Type I restriction enzyme EcoKI M protein
PRO_0000088022

Regions

Region148 – 1536S-adenosyl-L-methionine binding By similarity
Region178 – 1803S-adenosyl-L-methionine binding By similarity

Sites

Binding site2161S-adenosyl-L-methionine By similarity

Secondary structure

1 ........................................................................... 529
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08957 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: D41C02203747C965

FASTA52959,307
        10         20         30         40         50         60 
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEAEYL PEGYRWDDLK 

        70         80         90        100        110        120 
SRIGQEQLQF YRKMLVHLGE DDKKLVQAVF HNVSTTITEP KQITALVSNM DSLDWYNGAH 

       130        140        150        160        170        180 
GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF TPRPLIKTII HLLKPQPREV VQDPAAGTAG 

       190        200        210        220        230        240 
FLIEADRYVK SQTNDLDDLD GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH 

       250        260        270        280        290        300 
GGAIRLGNTL GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL 

       310        320        330        340        350        360 
HPGGRAAVVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV KTNVLFFTKG 

       370        380        390        400        410        420 
TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTDEHLQP FERVYGEDPH GLSPRTEGEW 

       430        440        450        460        470        480 
SFNAEETEVA DSEENKNTDQ HLATSRWRKF SREWIRTAKS DSLDISWLKD KDSIDADSLP 

       490        500        510        520 
EPDVLAAEAM GELVQALSEL DALMRELGAS DEADLQRQLL EEAFGGVKE

« Hide

References

« Hide 'large scale' references
[1]"Organization and sequence of the hsd genes of Escherichia coli K-12."
Loenen W.A.M., Daniel A.S., Braymer H.D., Murray N.E.
J. Mol. Biol. 198:159-170(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X06545 Genomic DNA. Translation: CAA29792.1.
U14003 Genomic DNA. Translation: AAA97246.1.
U00096 Genomic DNA. Translation: AAC77305.1.
AP009048 Genomic DNA. Translation: BAE78339.1.
PIRXYECHM. B30375.
RefSeqNP_418769.1. NC_000913.2.
YP_492480.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AR0X-ray2.80A/B2-527[»]
2Y7Celectron microscopy18.00B/C1-529[»]
2Y7Helectron microscopy18.00B/C1-529[»]
ProteinModelPortalP08957.
SMRP08957. Positions 1-529.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9943N.
IntActP08957. 14 interactions.
MINTMINT-1252160.
STRING511145.b4349.

Protein family/group databases

REBASE3387. M.EcoKI.

Proteomic databases

PaxDbP08957.
PRIDEP08957.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77305; AAC77305; b4349.
BAE78339; BAE78339; BAE78339.
GeneID12933774.
948872.
KEGGecj:Y75_p4234.
eco:b4349.
PATRIC32124304. VBIEscCol129921_4495.

Organism-specific databases

EchoBASEEB0453.
EcoGeneEG10458. hsdM.

Phylogenomic databases

eggNOGCOG0286.
HOGENOMHOG000295041.
KOK03427.
OMAIVQKLWN.
ProtClustDBCLSK891832.

Enzyme and pathway databases

BioCycEcoCyc:EG10458-MONOMER.
ECOL316407:JW4312-MONOMER.
MetaCyc:EG10458-MONOMER.

Gene expression databases

GenevestigatorP08957.

Family and domain databases

InterProIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
[Graphical view]
PfamPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08957.

Entry information

Entry nameT1MK_ECOLI
AccessionPrimary (citable) accession number: P08957
Secondary accession number(s): Q2M5W7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents