ID   T1RP_ECOLX              Reviewed;         313 AA.
AC   P17224;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Type I restriction enzyme EcoprrI endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=EcoprrI {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
GN   Name=prrD {ECO:0000303|PubMed:1691706};
GN   Synonyms=orfD {ECO:0000303|PubMed:1691706};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=CTR5X;
RX   PubMed=1691706; DOI=10.1002/j.1460-2075.1990.tb08253.x;
RA   Levitz R., Chapman D., Amitsur M., Green R., Snyder L., Kaufmann G.;
RT   "The optional E. coli prr locus encodes a latent form of phage T4-induced
RT   anticodon nuclease.";
RL   EMBO J. 9:1383-1389(1990).
RN   [2]
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).
CC   -!- FUNCTION: The subtype C restriction (R) subunit of a type I restriction
CC       enzyme that recognizes 5'-CCAN(7)RTGC-3' and cleaves a random distance
CC       away. The R subunit is required for both endonuclease and ATPase
CC       activities but not for modification. Cleaves only non-methylated DNA,
CC       hemi-methylated and fully methylated DNA are not substrates. After
CC       locating a non-methylated recognition site, the enzyme complex serves
CC       as a molecular motor that translocates DNA in an ATP-dependent manner
CC       until a collision occurs that triggers cleavage (PubMed:12654995) (By
CC       similarity). The prr locus restricts phage T4 mutants lacking
CC       polynucleotide kinase or RNA ligase; T4 mutants lacking these genes
CC       manifest a T4-induced anticodon nuclease (ACNase). This is a putative
CC       'masking-agent' for the ACNase encoded by prrC. It is thought that Stp
CC       and other T4-encoded ACNase factors counteract the masking agents, thus
CC       activating the latent ACNase (PubMed:1691706) (Probable).
CC       {ECO:0000250|UniProtKB:P08956, ECO:0000269|PubMed:1691706,
CC       ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1691706}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC         fragments with terminal 5'-phosphates, ATP is simultaneously
CC         hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000250|UniProtKB:P08956};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S; the restriction enzyme has stoichiometry
CC       R(2)M(2)S(1) while the methyltransferase is M(2)S(1).
CC       {ECO:0000250|UniProtKB:P08956}.
CC   -!- DISRUPTION PHENOTYPE: Manifests the latent anticodon nuclease (prrC,
CC       ACNase). {ECO:0000269|PubMed:1691706}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}.
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DR   EMBL; X52284; CAA36528.1; -; Genomic_DNA.
DR   PIR; S09628; S09628.
DR   AlphaFoldDB; P17224; -.
DR   SMR; P17224; -.
DR   REBASE; 2541; EcoprrI.
DR   PRIDE; P17224; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   Pfam; PF04313; HSDR_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Restriction system.
FT   CHAIN           1..313
FT                   /note="Type I restriction enzyme EcoprrI endonuclease
FT                   subunit"
FT                   /id="PRO_0000077261"
SQ   SEQUENCE   313 AA;  37036 MW;  FB2628D6630ED828 CRC64;
     MVDCTKPIAE SNNFIILDKY NPDWKITESY QSEGDLEREL IQDLVNQGYE YLPTLNNTKA
     MLANVREQLQ NLNNVEFLEA EWRRFVETWM DKPSDGVVEK ARKIHDDYVH DFVFDDGRIQ
     NIYLLDRKNI LRNKVQVIKQ FEQAGTHANR YDVTILVNGL PLVQIELKKR GVAIREAFNQ
     IHRYSKESFN SENSLFKYLQ LFVISNGTDT RYFANTTKRD KNSFDFTMNW AKSDNTLIKD
     LKDFTATFFQ KHTLLNVLVN YSVFDSSQTL LVMRPYQIAA TERILWKIKS SFTSEELVKT
     GKRWVYLAHY RFW