ID   E1Q2I5_HELPP            Unreviewed;      1000 AA.
AC   E1Q2I5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE            Short=R protein {ECO:0000256|RuleBase:RU364115};
DE            EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN   OrderedLocusNames=HPPC_04285 {ECO:0000313|EMBL:ADO07083.1};
OS   Helicobacter pylori (strain PeCan4).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=765963 {ECO:0000313|EMBL:ADO07083.1, ECO:0000313|Proteomes:UP000006863};
RN   [1] {ECO:0000313|Proteomes:UP000006863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PeCan4 {ECO:0000313|Proteomes:UP000006863};
RA   Kersulyte D., Vasquez J., Gilman R.H., Berg D.E.;
RT   "Complete genome sequence of Helicobacter pylori strain PeCan4.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC       activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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:0000256|ARBA:ARBA00000851,
CC         ECO:0000256|RuleBase:RU364115};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC       ECO:0000256|RuleBase:RU364115}.
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DR   EMBL; CP002074; ADO07083.1; -; Genomic_DNA.
DR   RefSeq; WP_001105668.1; NC_014555.1.
DR   AlphaFoldDB; E1Q2I5; -.
DR   REBASE; 28149; Hpy4ORF4291P.
DR   KEGG; hpc:HPPC_04285; -.
DR   HOGENOM; CLU_004848_1_0_7; -.
DR   Proteomes; UP000006863; Chromosome.
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   CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR   Gene3D; 1.20.58.2040; -; 1.
DR   Gene3D; 3.90.1570.50; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR   InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR   InterPro; IPR040980; SWI2_SNF2.
DR   InterPro; IPR022625; TypeI_RM_Rsu_C.
DR   NCBIfam; TIGR00348; hsdR; 1.
DR   PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR   PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR   Pfam; PF12008; EcoR124_C; 1.
DR   Pfam; PF04313; HSDR_N; 1.
DR   Pfam; PF18766; SWI2_SNF2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364115};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          300..463
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1000 AA;  116765 MW;  87E6806AFB953F04 CRC64;
     MNYETIAESN ESTVVAQFHS DSERKGAYES EAELERAFIA LLEKQGYEFK QIHNEKELKD
     NLKEQLEKLN DHCFTPKEWD TLYFQFIANK NDDYKAKTKK IQEDPIFNLT LENGKTKNIK
     IIDKKNIHRN ALQVIHQYSN KGGKYQNRYD VSILVNGLPL VHVELKKRGV AIREAFNQIK
     RYKRDSFSAE DGLFEFVQIF VISNGTSSKY YSNTTRIAQI EKNNKADTFE FTNYWADSKN
     HNIEDLMDFA QSFFAKRSLL NVLTRYCVFT SDEVLLVMRP YQIVAAERIL EKIKATQNSK
     TYKKSQNGGY IWHTTGSGKT LTSFKSAALA KELEGISKVL FVVDRKDLDY QTMKEYDKFQ
     KDCANSNTST KILKEQLEDS NAKIIITTIQ KLDKFVKAHS KGHAIFNEEV VMIFDECHRS
     QLGLMHQAIT KAFKKYHLFG FTGTPIFAQN CDKNNPLGTT EQKFGKCLHQ YTIIDAIRDK
     NVLPFRVEYH NTIKAKEDIK DKEVRAVDEK NALLDSRRIK EITKCILERF NQATKNKKFN
     SILACQNIEA LKKYYQAFKE EKHDLKIATI FSYSANEEIE ALEDENNESA AGLDKSSRDF
     LEGAIADYNG MFKTSFDTSD QKFQSYYKDL SQKMKDRKID LLMVVNMFLT GFDATRLNTL
     WVDKNLKYHG LIQAFSRANR ILDSVKTHGN IVCFRDLEQD LNDALMLFGN KDAQSIALLR
     KYEDYLKGYV DNNKEYEGYE GLIERLLTEF PLKEPIISES QKKDFIKLFG KILKLENILN
     SFENFNKDDH INPRDFQDYQ SKYLDFYDEM RPEKGRDKEE INDDLIFEIE LIKQVEVNID
     YILNLIEKFA KEHGVEIQGV KTKIEPILNS SIELRNKRDL IMGFIDKYNK DQEVHAHFQD
     YIHQKREEEF QDIIKENRLN EEKAYSFMQH AFKGGEISFS GTEFPKIIEE KPSMFSQNSR
     YQEVKEKVAA SLSRFFHRFC DLTSAIFKKN GVKKDEVNEK
//