Type I restriction enzyme EcoKI M protein - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P08957 (T1MK_ECOLI)

Last modified November 3, 2009. Version 90. 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:
    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

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	529 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	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.

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Ontologies

Keywords
Biological process	Restriction system
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA methylation Inferred from electronic annotation. Source: InterPro DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro N-methyltransferase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct site-specific DNA-methyltransferase (adenine-specific) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ung	P12295	1	EBI-878571,EBI-559403

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 529

529

Type I restriction enzyme EcoKI M protein

PRO_0000088022

Regions

Region

148 – 153

S-adenosyl-L-methionine binding By similarity

Region

178 – 180

S-adenosyl-L-methionine binding By similarity

Sites

Binding site

216

S-adenosyl-L-methionine By similarity

Secondary structure

529

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P08957-1 [UniParc].

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

529

59,307

        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

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References

	« Hide 'large scale' referencesShow '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: 3323532] [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: 7610040] [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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

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Cross-references

Sequence databases

X06545 Genomic DNA. Translation: CAA29792.1.
U14003 Genomic DNA. Translation: AAA97246.1.
U00096 Genomic DNA. Translation: AAC77305.1.
AP009048 Genomic DNA. Translation: BAE78339.1.

PIR

XYECHM. B30375.

RefSeq

AP_004838.1.
NP_418769.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AR0	X-ray	2.80	A/B	2-527	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P08957. 14 interactions.

STRING

P08957.

Protein family/group databases

REBASE

3387. M.EcoKI.

2-D gel databases

ECO2DBASE

C059.3. 6TH EDITION.
C059.4. 6TH EDITION.

Genome annotation databases

GeneID

948872.

GenomeReviews

Gene locus JW4312 in contig AP009048_GR.
Gene locus b4349 in contig U00096_GR.

KEGG

ecj:JW4312.
eco:b4349.

Organism-specific databases

EchoBASE

EB0453.

EcoGene

EG10458. hsdM.

CMR

Search...

Phylogenomic databases

HOGENOM

P08957.

OMA

NAEDTKS.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10458-MON.

Gene expression databases

Genevestigator

P08957.

Family and domain databases

InterPro

IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
[Graphical view]

Pfam

PF02384. N6_Mtase. 1 hit.
[Graphical view]

PRINTS

PR00507. N12N6MTFRASE.

PROSITE

PS00092. N6_MTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

T1MK_ECOLI

Accession

Primary (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:	November 3, 2009
This is version 90 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

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

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

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents