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P08957

- T1MK_ECOLI

UniProt

P08957 - T1MK_ECOLI

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Protein

Type I restriction enzyme EcoKI M protein

Gene

hsdM

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei216 – 2161S-adenosyl-L-methionineBy similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. N-methyltransferase activity Source: EcoliWiki
  3. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

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

Protein family/group databases

REBASEi3387. M.EcoKI.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme EcoKI M protein (EC:2.1.1.72)
Short name:
M.EcoKI
Gene namesi
Name:hsdM
Synonyms:hsm
Ordered Locus Names:b4349, JW4312
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10458. hsdM.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Type I restriction enzyme EcoKI M proteinPRO_0000088022Add
BLAST

Proteomic databases

PaxDbiP08957.
PRIDEiP08957.

Expressioni

Gene expression databases

GenevestigatoriP08957.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-9943N.
IntActiP08957. 14 interactions.
MINTiMINT-1252160.
STRINGi511145.b4349.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814
Turni19 – 213
Helixi27 – 4317
Helixi46 – 494
Helixi56 – 605
Helixi64 – 7815
Beta strandi80 – 823
Helixi84 – 907
Helixi100 – 11112
Helixi153 – 16311
Beta strandi171 – 1733
Turni177 – 1793
Helixi180 – 19011
Turni191 – 1988
Helixi201 – 2099
Beta strandi211 – 2177
Helixi219 – 23012
Turni231 – 2333
Helixi238 – 2403
Beta strandi242 – 2476
Helixi252 – 2554
Beta strandi260 – 2656
Helixi288 – 29912
Beta strandi300 – 31112
Helixi312 – 3165
Helixi320 – 33112
Beta strandi332 – 3398
Beta strandi345 – 3473
Beta strandi352 – 3609
Beta strandi374 – 3796
Beta strandi388 – 3914
Helixi395 – 3973
Helixi399 – 4057
Beta strandi427 – 4293
Helixi433 – 4353
Helixi442 – 4443
Beta strandi446 – 4516
Helixi452 – 4576
Beta strandi459 – 4613
Helixi482 – 50524
Helixi511 – 52111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AR0X-ray2.80A/B2-527[»]
2Y7Celectron microscopy18.00B/C1-529[»]
2Y7Helectron microscopy18.00B/C1-529[»]
ProteinModelPortaliP08957.
SMRiP08957. Positions 1-529.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08957.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1536S-adenosyl-L-methionine bindingBy similarity
Regioni178 – 1803S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0286.
HOGENOMiHOG000295041.
InParanoidiP08957.
KOiK03427.
OMAiCDVLRDD.
OrthoDBiEOG686NCV.
PhylomeDBiP08957.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08957-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEAEYL
60 70 80 90 100
PEGYRWDDLK SRIGQEQLQF YRKMLVHLGE DDKKLVQAVF HNVSTTITEP
110 120 130 140 150
KQITALVSNM DSLDWYNGAH GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF
160 170 180 190 200
TPRPLIKTII HLLKPQPREV VQDPAAGTAG FLIEADRYVK SQTNDLDDLD
210 220 230 240 250
GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH GGAIRLGNTL
260 270 280 290 300
GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL
310 320 330 340 350
HPGGRAAVVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV
360 370 380 390 400
KTNVLFFTKG TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTDEHLQP
410 420 430 440 450
FERVYGEDPH GLSPRTEGEW SFNAEETEVA DSEENKNTDQ HLATSRWRKF
460 470 480 490 500
SREWIRTAKS DSLDISWLKD KDSIDADSLP EPDVLAAEAM GELVQALSEL
510 520
DALMRELGAS DEADLQRQLL EEAFGGVKE
Length:529
Mass (Da):59,307
Last modified:November 1, 1988 - v1
Checksum:iD41C02203747C965
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06545 Genomic DNA. Translation: CAA29792.1.
U14003 Genomic DNA. Translation: AAA97246.1.
U00096 Genomic DNA. Translation: AAC77305.1.
AP009048 Genomic DNA. Translation: BAE78339.1.
PIRiB30375. XYECHM.
RefSeqiNP_418769.1. NC_000913.3.
YP_492480.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77305; AAC77305; b4349.
BAE78339; BAE78339; BAE78339.
GeneIDi12933774.
948872.
KEGGiecj:Y75_p4234.
eco:b4349.
PATRICi32124304. VBIEscCol129921_4495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06545 Genomic DNA. Translation: CAA29792.1 .
U14003 Genomic DNA. Translation: AAA97246.1 .
U00096 Genomic DNA. Translation: AAC77305.1 .
AP009048 Genomic DNA. Translation: BAE78339.1 .
PIRi B30375. XYECHM.
RefSeqi NP_418769.1. NC_000913.3.
YP_492480.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AR0 X-ray 2.80 A/B 2-527 [» ]
2Y7C electron microscopy 18.00 B/C 1-529 [» ]
2Y7H electron microscopy 18.00 B/C 1-529 [» ]
ProteinModelPortali P08957.
SMRi P08957. Positions 1-529.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9943N.
IntActi P08957. 14 interactions.
MINTi MINT-1252160.
STRINGi 511145.b4349.

Protein family/group databases

REBASEi 3387. M.EcoKI.

Proteomic databases

PaxDbi P08957.
PRIDEi P08957.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77305 ; AAC77305 ; b4349 .
BAE78339 ; BAE78339 ; BAE78339 .
GeneIDi 12933774.
948872.
KEGGi ecj:Y75_p4234.
eco:b4349.
PATRICi 32124304. VBIEscCol129921_4495.

Organism-specific databases

EchoBASEi EB0453.
EcoGenei EG10458. hsdM.

Phylogenomic databases

eggNOGi COG0286.
HOGENOMi HOG000295041.
InParanoidi P08957.
KOi K03427.
OMAi CDVLRDD.
OrthoDBi EOG686NCV.
PhylomeDBi P08957.

Enzyme and pathway databases

BioCyci EcoCyc:EG10458-MONOMER.
ECOL316407:JW4312-MONOMER.
MetaCyc:EG10458-MONOMER.

Miscellaneous databases

EvolutionaryTracei P08957.
PROi P08957.

Gene expression databases

Genevestigatori P08957.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00507. N12N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiT1MK_ECOLI
AccessioniPrimary (citable) accession number: P08957
Secondary accession number(s): Q2M5W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 29, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

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. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3