T3RE_BPP1
ID T3RE_BPP1 Reviewed; 970 AA.
AC P08764;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Type III restriction-modification enzyme EcoPI Res subunit;
DE EC=3.1.21.5 {ECO:0000269|PubMed:11178902};
DE AltName: Full=Type III restriction enzyme EcoPI {ECO:0000303|PubMed:12654995};
GN Name=res {ECO:0000303|PubMed:2837577};
OS Escherichia phage P1 (Bacteriophage P1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Punavirus.
OX NCBI_TaxID=2886926;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT "Genome of bacteriophage P1.";
RL J. Bacteriol. 186:7032-7068(2004).
RN [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF ARG-534; PRO-897; ASP-898; GLU-916 AND LYS-918.
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.
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).
CC -!- FUNCTION: A type III restriction enzyme that recognizes 2 inversely
CC oriented double-stranded sequences 5'-AGACC-3' and cleaves DNA 25-27
CC base pairs downstream of one site, producing a single-strand 5'
CC protrusion of two nucleotides. DNA restriction requires both the Res
CC and Mod subunits (PubMed:2837577, PubMed:11178902). DNA topology
CC affects its action; relaxed and negatively supercoiled DNA are digested
CC but positively supercoiled DNA is not a good substrate
CC (PubMed:11178902). After binding to one recognition site undergoes
CC random one-dimensional diffusion along DNA until it collides with a
CC stationary enzyme bound to the second DNA site, which is when DNA
CC cleavage occurs (By similarity). {ECO:0000250|UniProtKB:Q5ZND2,
CC ECO:0000269|PubMed:11178902, ECO:0000269|PubMed:2837577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.5;
CC Evidence={ECO:0000269|PubMed:11178902};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000269|PubMed:11178902};
CC -!- SUBUNIT: A heterotetramer with stoichiometry Res(2)Mod(2).
CC {ECO:0000269|PubMed:11178902}.
CC -!- DOMAIN: Has a helicase-type domain in its N-terminus and an
CC endonuclease-type domain in its C-terminus; ATP and DNA hydrolysis
CC activities are mediated by the N- and C-terminal domains respectively.
CC The C-terminus is probably required for interaction with the Mod
CC subunit; deletion of residues 897-970 is unstable as is this protein
CC when expressed alone. {ECO:0000269|PubMed:11178902}.
CC -!- MISCELLANEOUS: This R-M system is also known as EcoP1 and EcoP1I.
CC {ECO:0000303|PubMed:11178902, ECO:0000303|PubMed:2837577}.
CC -!- SIMILARITY: Belongs to the type III restriction-modification system Res
CC protein family. {ECO:0000305}.
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DR EMBL; X06287; CAA29615.1; -; Genomic_DNA.
DR EMBL; AF234172; AAQ13982.1; -; Genomic_DNA.
DR PIR; S01352; S01352.
DR RefSeq; YP_006476.1; NC_005856.1.
DR SMR; P08764; -.
DR REBASE; 7754; EphP1ORF1P.
DR REBASE; 988; EcoPI.
DR GeneID; 2777489; -.
DR KEGG; vg:2777489; -.
DR BRENDA; 3.1.21.5; 16473.
DR PRO; PR:P08764; -.
DR Proteomes; UP000008091; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0015668; F:type III site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR045572; RE_endonuc_C.
DR Pfam; PF19778; RE_endonuc; 1.
DR Pfam; PF04851; ResIII; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Endonuclease; Helicase; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine.
FT CHAIN 1..970
FT /note="Type III restriction-modification enzyme EcoPI Res
FT subunit"
FT /id="PRO_0000077374"
FT REGION 75..540
FT /note="Helicase-like domain"
FT /evidence="ECO:0000269|PubMed:11178902"
FT REGION 894..918
FT /note="Endonuclease domain"
FT /evidence="ECO:0000269|PubMed:11178902"
FT MUTAGEN 534
FT /note="R->A: No DNA restriction, no ATPase activity, forms
FT wild-type complex with Mod."
FT /evidence="ECO:0000269|PubMed:11178902"
FT MUTAGEN 897
FT /note="P->A: Wild-type DNA restriction."
FT /evidence="ECO:0000269|PubMed:11178902"
FT MUTAGEN 898
FT /note="D->A: No DNA restriction, wild-type ATPase, forms
FT wild-type complex with Mod."
FT /evidence="ECO:0000269|PubMed:11178902"
FT MUTAGEN 916
FT /note="E->A: No DNA restriction, has some single-strand
FT nicking activity, wild-type ATPase, forms wild-type complex
FT with Mod."
FT /evidence="ECO:0000269|PubMed:11178902"
FT MUTAGEN 918
FT /note="K->A: No DNA restriction, wild-type ATPase, forms
FT wild-type complex with Mod."
FT /evidence="ECO:0000269|PubMed:11178902"
SQ SEQUENCE 970 AA; 111459 MW; B599110154D723AA CRC64;
MSKGFTFEKN LPHQKAGVDA VMNVFVSATS HQEDNVSIRL LVNPELRLTE QQYYKNIKKV
QELNGIEHVK NNYDARSNVI DVSMETGTGK TYTYTKTIFD LNKSFGINKF IIIVPTLSIK
AGTVNFLKSD ALKEHFRDDY EREIKTYVVE SQKNAGKSTK SYMPQAIHDF VEASNFNKKY
IHVLVINTGM IHSKNLNSTY DVGLLDNHFD SPFSALGAVK PFIIIDEPHK FPTGKKTWEN
IEKFNAQYII RYGATFSEGY KNLVYRLTAV DAFNEDLVKG IDAYIEDIVG DGDANLKFIK
SDGEEVTFEL NENNKKTLFK LTKGESLSKT HSAIHDLTLD ALGKNTVVLS NGIELKIGCS
INPYSYDQTL ADSMMRKAIK EHFKLEKEFL TQRPRIKPLT LFFIDDIEGY RDGNNIAGSL
KAKFEEYVLA EANELLKIEK DEFYSNYLEK TVKDISSVHG GYFSKDNSDK DDKIEKEINE
ILHDKELLLS LDNPRRFIFS KWTLREGWDN PNVFQICKLR SSGSTTSKLQ EVGRGLRLPV
NEYMCRVKDR NFTLKYYVDF TEKDFVDSLV KEVNESSFKE RVPSKFTQEL KEQIRAQYPE
LSSRALMNEL FNDEIIDDND NFKDSDAYSR LKSKYPAAFP IGVKPGKIKK ATDGKRRTKM
RVGKFSELKE LWELINQKAV IEYKINSENE FLSIFKSFML EETERFTKSG VHTRIDKIYI
HNDMAMSKSI VSDDDDFAKL NTMSYREFLD NLSQTIFVKH DTLHKVFCDI KDTINITEYL
NIQTIRKIKS GFSKYLLNNS FNKFSLGYNL ISGSIHPTKF TNADGKPLDE VLSSDLGVLQ
DNSKAPLDTY LFEEVFYDSE LERRNITDRE IQSVVVFSKI PKNSIKIPVA GGYTYSPDFA
YVVKTAEGDY LNFIIETKNV DSKDSLRLEE KKKIEHAQAL FNQISQSVKV EFKTQFANDD
IYQLIKSALP
