T3MO_ECOLX
ID T3MO_ECOLX Reviewed; 644 AA.
AC P12364; Q5ZND1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Type III restriction-modification enzyme EcoP15I Mod subunit {ECO:0000303|PubMed:11178902};
DE Short=M.EcoP15I;
DE EC=2.1.1.72 {ECO:0000305|PubMed:26067164};
DE AltName: Full=EcoP15I methyltransferase;
DE AltName: Full=Type III methyltransferase M.EcoP15I {ECO:0000303|PubMed:12654995};
GN Name=mod {ECO:0000303|PubMed:2837577};
GN Synonyms=ecoP15Imod {ECO:0000303|PubMed:15464603};
OS Escherichia coli.
OG Plasmid p15B.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=p15B;
RX PubMed=2837577; DOI=10.1016/0022-2836(88)90330-0;
RA Huembelin M., Suri B., Rao D.N., Hornby D.P., Eberle H., Pripfl T.,
RA Kenel S., Bickle T.A.;
RT "Type III DNA restriction and modification systems EcoP1 and EcoP15.
RT Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1
RT mod mutants.";
RL J. Mol. Biol. 200:23-29(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 156; 343; 472
RP AND 513.
RC PLASMID=p15B;
RX PubMed=15464603; DOI=10.1016/j.jbiotec.2004.06.014;
RA Moencke-Buchner E., Mackeldanz P., Krueger D.H., Reuter M.;
RT "Overexpression and affinity chromatography purification of the Type III
RT restriction endonuclease EcoP15I for use in transcriptome analysis.";
RL J. Biotechnol. 114:99-106(2004).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11178902; DOI=10.1006/jmbi.2000.4411;
RA Janscak P., Sandmeier U., Szczelkun M.D., Bickle T.A.;
RT "Subunit assembly and mode of DNA cleavage of the type III restriction
RT endonucleases EcoP1I and EcoP15I.";
RL J. Mol. Biol. 306:417-431(2001).
RN [4]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
RN [5] {ECO:0007744|PDB:4ZCF}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RES AND DNA.
RX PubMed=26067164; DOI=10.1038/ncomms8363;
RA Gupta Y.K., Chan S.H., Xu S.Y., Aggarwal A.K.;
RT "Structural basis of asymmetric DNA methylation and ATP-triggered long-
RT range diffusion by EcoP15I.";
RL Nat. Commun. 6:7363-7363(2015).
CC -!- FUNCTION: A beta subtype methylase that binds the system-specific DNA
CC recognition site 5'-CAGCAG-3' and methylates A-5 (of only 1 strand as
CC the other does not have an A residue). DNA restriction requires both
CC the Res and Mod subunits (PubMed:11178902, PubMed:12654995). The A-5
CC nucleotide flips into the catalytic pocket of one Mod subunit for
CC modification, while the other Mod subunit makes most of the DNA
CC sequence-specific contacts (PubMed:26067164).
CC {ECO:0000269|PubMed:11178902, ECO:0000269|PubMed:26067164,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000305|PubMed:26067164};
CC -!- SUBUNIT: Forms a homodimer capable of methylating the target sequence
CC in the absence of Res (Probable). A heterotetramer with stoichiometry
CC Res(2)Mod(2) (PubMed:11178902). A heterotrimer with stoichiometry
CC Res(1)Mod(2) (PubMed:26067164). {ECO:0000269|PubMed:11178902,
CC ECO:0000269|PubMed:26067164, ECO:0000305|PubMed:26067164}.
CC -!- MISCELLANEOUS: This R-M system is also called EcoP15.
CC {ECO:0000303|PubMed:2837577}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X06288; CAA29616.1; -; Genomic_DNA.
DR EMBL; AJ634453; CAG24072.1; -; Genomic_DNA.
DR PIR; S03208; S03208.
DR PDB; 4ZCF; X-ray; 2.60 A; A/B=1-644.
DR PDBsum; 4ZCF; -.
DR AlphaFoldDB; P12364; -.
DR REBASE; 3389; M.EcoP15I.
DR BRENDA; 3.1.21.5; 2026.
DR PRO; PR:P12364; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041405; T3RM_EcoP15I_C.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18273; T3RM_EcoP15I_C; 1.
DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR PRINTS; PR00506; D21N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..644
FT /note="Type III restriction-modification enzyme EcoP15I Mod
FT subunit"
FT /id="PRO_0000088031"
FT REGION 123..126
FT /note="Binding of S-adenosyl methionine"
FT /evidence="ECO:0000255"
FT CONFLICT 156
FT /note="E -> Q (in Ref. 1; CAA29616)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="K -> KQ (in Ref. 1; CAA29616)"
FT /evidence="ECO:0000305"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:4ZCF"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:4ZCF"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:4ZCF"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:4ZCF"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4ZCF"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 420..430
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 431..441
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 461..468
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 487..500
FT /evidence="ECO:0007829|PDB:4ZCF"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 539..552
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 562..566
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 587..598
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 606..611
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:4ZCF"
FT HELIX 618..629
FT /evidence="ECO:0007829|PDB:4ZCF"
FT STRAND 639..643
FT /evidence="ECO:0007829|PDB:4ZCF"
SQ SEQUENCE 644 AA; 74094 MW; 01B84990BCD43A41 CRC64;
MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE LSKESYSLNW
LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQHLLIKG DNLEVLKHMV NAYAEKVKMI
YIDPPYNTGK DGFVYNDDRK FTPEQLSELA GIDLDEAKRI LEFTTKGSSS HSAWLTFIYP
RLYIARELMR EDGTIFISID HNEFSQLKLV CDEIFGEQNH VGDLVWKNAT DNNPSNIAVE
HEYIIVYTKN KEQLISEWKS NISDVKNLLV NIGEEFASKY TGNELQEKYT QWFREHRSEL
WPLDRYKYID KDGIYTGSQS VHNPGKEGYR YDIIHPKTKK PCKQPLMGYR FPLDTMDRLL
SEEKIIFGDD ENKIIELKVY AKDYKQKLSS VIHLDGRVAT NELKELFPEM TQPFTNAKTI
KLVEDLISFA CDGEGIVLDF FAGSGTTAHT VFNLNNKNKT SYQFITVQLD EPTKDKSDAM
KHGYNTIFDL TKERLIRASK KNRDQGFKVY QLMPDFRAKD ESELTLSNHT FFDDVVLTPE
QYDTLLTTWC LYDGSLLTTP IEDVDLGGYK AHLCDGRLYL IAPNFTSEAL KALLQKVDSD
KDFAPNKVVF YGSNFESAKQ MELNEALKSY ANKKSIELDL VVRN
