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P08957

- T1MK_ECOLI

UniProt

P08957 - T1MK_ECOLI

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
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    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

    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.
    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.
    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

    MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEAEYL    50
    PEGYRWDDLK SRIGQEQLQF YRKMLVHLGE DDKKLVQAVF HNVSTTITEP 100
    KQITALVSNM DSLDWYNGAH GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF 150
    TPRPLIKTII HLLKPQPREV VQDPAAGTAG FLIEADRYVK SQTNDLDDLD 200
    GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH GGAIRLGNTL 250
    GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL 300
    HPGGRAAVVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV 350
    KTNVLFFTKG TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTDEHLQP 400
    FERVYGEDPH GLSPRTEGEW SFNAEETEVA DSEENKNTDQ HLATSRWRKF 450
    SREWIRTAKS DSLDISWLKD KDSIDADSLP EPDVLAAEAM GELVQALSEL 500
    DALMRELGAS DEADLQRQLL EEAFGGVKE 529
    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.
    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.
    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

    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 1, 2014
    This is version 128 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