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   27-MAR-2024, entry version 104.
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   Punavirus; Punavirus P1.
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; 615499; EphP1ORFAP.
DR   REBASE; 7754; EphP1ORF1P.
DR   REBASE; 988; EcoPI.
DR   GeneID; 2777489; -.
DR   KEGG; vg:2777489; -.
DR   OrthoDB; 2580at10239; -.
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; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR045572; RE_endonuc_C.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF19778; RE_endonuc; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//