ID   B6JPJ3_HELP2            Unreviewed;       258 AA.
AC   B6JPJ3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN   OrderedLocusNames=HPP12_0094 {ECO:0000313|EMBL:ACJ07254.1};
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508 {ECO:0000313|EMBL:ACJ07254.1, ECO:0000313|Proteomes:UP000008198};
RN   [1] {ECO:0000313|Proteomes:UP000008198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12 {ECO:0000313|Proteomes:UP000008198};
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACJ07254.1, ECO:0000313|Proteomes:UP000008198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12 {ECO:0000313|EMBL:ACJ07254.1,
RC   ECO:0000313|Proteomes:UP000008198};
RX   PubMed=20478826; DOI=10.1093/nar/gkq378;
RA   Fischer W., Windhager L., Rohrer S., Zeiller M., Karnholz A., Hoffmann R.,
RA   Zimmer R., Haas R.;
RT   "Strain-specific genes of Helicobacter pylori: genome evolution driven by a
RT   novel type IV secretion system and genomic island transfer.";
RL   Nucleic Acids Res. 38:6089-6101(2010).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded unmethylated sequence 5'-GATC-3'.
CC       {ECO:0000256|PIRNR:PIRNR016080}.
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:0000256|PIRNR:PIRNR016080};
CC   -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease
CC       family. {ECO:0000256|PIRNR:PIRNR016080}.
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DR   EMBL; CP001217; ACJ07254.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6JPJ3; -.
DR   REBASE; 19174; HpyPIIIP.
DR   KEGG; hpp:HPP12_0094; -.
DR   HOGENOM; CLU_089327_0_0_7; -.
DR   Proteomes; UP000008198; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.91.80; -; 1.
DR   InterPro; IPR038365; EcoRII_C_sf.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR021191; Restrct_endonuc_II_DpnII.
DR   InterPro; IPR007637; Restrct_endonuc_II_DpnII-like.
DR   Pfam; PF04556; DpnII; 1.
DR   PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:ACJ07254.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR016080};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT   DOMAIN          7..249
FT                   /note="Restriction endonuclease type II DpnII-like"
FT                   /evidence="ECO:0000259|Pfam:PF04556"
SQ   SEQUENCE   258 AA;  30159 MW;  7015CE51D4244D8B CRC64;
     MKNRLPFDTF LKSLKTSNRT LDFFTDWQKC LKNKNEISIA LNHLNFLLGK DTKELKNCIK
     SLFKEYPKAF DVLNILIAVR DKDDIVRDAN GNFYPLHSYF ENDEKVYEFI CQTGLEQIFC
     NRNIKDLNDF VFGIEVGLDS NARKNRSGKA MENHLSGLFV QAQLNFKEQV DIREFKDLCQ
     AFGNDIKKFD FVIFGKNKTY FIEANFYTIS GSKLNEVARS YQDLALKFEA FPNYEFIWIT
     MAQVGWTLKT NSKKLTNL
//