T257_ECOLX
ID T257_ECOLX Reviewed; 998 AA.
AC P25239;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Type II restriction enzyme and methyltransferase RM.Eco57I {ECO:0000303|PubMed:12654995};
DE EC=3.1.21.4 {ECO:0000269|PubMed:1334260};
DE AltName: Full=Endonuclease Eco57I;
DE AltName: Full=Type IIS restriction enzyme Eco57I;
DE Includes:
DE RecName: Full=Adenine-specific methyltransferase activity Eco57IA;
DE Short=M.Eco57IA;
DE EC=2.1.1.72 {ECO:0000269|PubMed:1334260};
GN Name=eco57IR {ECO:0000303|PubMed:1334261};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, AND FUNCTION.
RC STRAIN=RFL57;
RX PubMed=1334261; DOI=10.1093/nar/20.22.6051;
RA Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V.;
RT "Cloning and sequence analysis of the genes coding for Eco57I type IV
RT restriction-modification enzymes.";
RL Nucleic Acids Res. 20:6051-6056(1992).
RN [2]
RP NOMENCLATURE, AND SUBTYPES.
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 [3]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) IN COMPLEX WITH DNA, AND SEQUENCE
RP REVISION.
RX PubMed=15134658; DOI=10.1016/j.bbapap.2003.12.006;
RA Tamulaitiene G., Grazulis S., Janulaitis A., Janowski R., Bujacz G.,
RA Jaskolski M.;
RT "Crystallization and preliminary crystallographic studies of a bifunctional
RT restriction endonuclease Eco57I.";
RL Biochim. Biophys. Acta 1698:251-254(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=1334260; DOI=10.1093/nar/20.22.6043;
RA Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V.;
RT "Purification and properties of the Eco57I restriction endonuclease and
RT methylase -- prototypes of a new class (type IV).";
RL Nucleic Acids Res. 20:6043-6049(1992).
CC -!- FUNCTION: An E, G and S subtype restriction enzyme that recognizes the
CC (non-palindromic) double-stranded sequence 5'-CTGAAG-3' and cleaves
CC respectively 22 bases after C-1 and 14 bases before C'-1; cleavage of
CC lambda DNA is never complete. Also acts as a methylase that causes
CC specific methylation on A-5 in 5'-CTGAAG-3', the other strand is
CC methylated by the M.Eco57I methylase. {ECO:0000269|PubMed:1334260,
CC ECO:0000269|PubMed:1334261, ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000269|PubMed:1334260};
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:0000269|PubMed:1334260};
CC -!- ACTIVITY REGULATION: Mg(2+) is absolutely required for DNA restriction.
CC {ECO:0000269|PubMed:1334260}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0 for DNA restriction and 7.5 for methylation.
CC {ECO:0000269|PubMed:1334260};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:1334260}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the N(4)/N(6)-
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; M74821; AAA23389.1; -; Genomic_DNA.
DR EMBL; X61122; CAA43434.3; -; Genomic_DNA.
DR PIR; S26426; S26426.
DR AlphaFoldDB; P25239; -.
DR SMR; P25239; -.
DR REBASE; 941; Eco57I.
DR PRIDE; P25239; -.
DR BRENDA; 3.1.21.4; 2026.
DR PRO; PR:P25239; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease 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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; RM_methylase_Eco57I-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07669; Eco57I; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Endonuclease; Hydrolase;
KW Methyltransferase; Multifunctional enzyme; Nuclease; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..998
FT /note="Type II restriction enzyme and methyltransferase
FT RM.Eco57I"
FT /id="PRO_0000077274"
FT CONFLICT 42
FT /note="I -> L (in Ref. 1; AAA23389)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="R -> G (in Ref. 1; AAA23389)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..321
FT /note="WSIIEQLYFPQSTYSFSVFSSDI -> EHHRTIILPHKAHTLSLFSLLIF
FT (in Ref. 1; AAA23389)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="E -> V (in Ref. 1; AAA23389)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="F -> N (in Ref. 1; AAA23389)"
FT /evidence="ECO:0000305"
FT CONFLICT 816..823
FT /note="PNEWYRYG -> LMMVQIR (in Ref. 1; AAA23389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 998 AA; 117087 MW; EDB090A7FBFFCC93 CRC64;
MNKKDQLQRL IDKYKSDIDY YRSARYNETQ LRTDFLDQLF LILGWDITNA AGKPTNEREV
LVEEGLKARA GENTKKPDYT FRLFSERKFF LEAKKPSVDI STTIEPALQV RRYGFTAKLK
ISVLSNFEYT AIYDCSNQVK ETDSVANSRI KLYHFTELVD KFDEINNLIG RESVYTGHFD
NEWSEIENKI LRFSVDDLFL KQINDWRLLL ANEFLQIKNE LPEEKLNDLV QNYINSIVFL
RVCEDRDLEE YETLYHFAQD KDFQSLVKKL KSSDKKYNSG LFSLEYIDEL LSNANSCIWS
IIEQLYFPQS TYSFSVFSSD ILGNIYEIFL SEKVRIDELG NVKIQPKEEH IDRDVVTTPT
HIVKEIIRNT VVEYCKGKSD IEILNSKFAD IACGSGAFII EAFQFIQDIL IDYYIQNDKS
KLQQISEHTY KLKFEVKREI LCKCIYGIDK DYNATKACTF GLLLKLLEGE TTETIGKDTP
ILPALDTNIL FGNSLIDSGD KVKQEDIFSI NPFDLTNYQF DVIVGNPPYM ATEHMNQLTP
KELDIYKRKY KSAYKQFDKY FLFIERSIQI LKEYGYLGYI LPSRFIKVDA GKKLRKFLSE
NKYLSKLISF GSHQVFKNKT TYTCLLFLNK ENHDNFSFYE VKDFKKWLTR EDKYLLSSTY
QTSSLDSDTW VLEKKINDIL KLMFSKSEQL GNIVGKSNVA NGIQTSANKY YIHKEIKSEN
GFIYFEYDGI EYHIEKELTR PYFETNRSGD DSFYTYKDVE PNSFVVYPYK KVGERIQFIE
YDELKRQYPK LFEFLQVVKV HLNDKKRSIK PDPTGPNEWY RYGRSQALEN CDVDQKLIVG
ILSNGYKYSI DNHRTFVSSG GTAGYSIINI PNNVRYSIYY IQAILTSKYL EWFASIYGDI
FRGRFVARGT KVQTRMPIPT IDFDDPKQKE IHDTISSKQQ YLNKLYSQTQ KSADRDKIIF
ERQFEQEKIQ MDYLIKNLFD LGDLDSEIPT VEDLYKNL
