ID J0NM43_HELPX Unreviewed; 991 AA.
AC J0NM43;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 Name=hsdR3 {ECO:0000313|EMBL:EJB87517.1};
GN ORFNames=HPHPH11_0137 {ECO:0000313|EMBL:EJB87517.1};
OS Helicobacter pylori Hp H-11.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992064 {ECO:0000313|EMBL:EJB87517.1, ECO:0000313|Proteomes:UP000004974};
RN [1] {ECO:0000313|EMBL:EJB87517.1, ECO:0000313|Proteomes:UP000004974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-11 {ECO:0000313|EMBL:EJB87517.1,
RC ECO:0000313|Proteomes:UP000004974};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJB87517.1}.
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DR EMBL; AKPC01000002; EJB87517.1; -; Genomic_DNA.
DR RefSeq; WP_000845638.1; NZ_AKPC01000002.1.
DR AlphaFoldDB; J0NM43; -.
DR PATRIC; fig|992064.3.peg.142; -.
DR Proteomes; UP000004974; Unassembled WGS sequence.
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; 3.90.1570.50; -; 1.
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 NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 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 251..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 991 AA; 115580 MW; 86B48C9CC386E8D7 CRC64;
MKTEKEVQKQ VIETFKAMGY AYLGDLTKSD NENINKESLK AWLIKNQKIE PERWHKIEQK
IHNALKNDLY EANQTFYELL IYGVNTKISQ NENTQTTWLI DWKDVSKNEF SVAEEVSVKG
PNAKRPDVVL YVNGIALGVL ELKKSSVSVE SGIRQNLDNQ KKEFIRDFFK TIQLVMAGNE
SQGLKYGVIE TKEKYYLSWK EEGVLKNLFE TIECFLKKER FLEFIHDFLI FDKGQKKCAR
FHQYFAIKKT QEFIKRKEGG IIWHTQGSGK SLTMVWLTRW LRRNTTQARV LIVTDRRELD
AQIQGVFEGI GEDLYRADSK KDLLSVLFEN KEFLVGSLVH KFDDNDLEDL KKQPVLKKWI
VLVDECHRTQ SAKLHKAMKS LLPNAIFIAF SGTPLLKQDK KTSQEVFGDY IHCYKFNEAV
SDKVVLDLNY EARSVDQYVS SPEKLDEYFE LKTQGLNEAA KTELKKKWVN LQKVFSTKDR
LARIVQDIVL DMAKLPRLRN GKGNAMLVAE SVYNACQYFE LFLETELKDK VAVITSYEPN
IADLKDCGSK ESEESYKYRT YCKMLQNFFN EKDEKKALNK IKEFEEEVKK RFINEPNRMK
LLIVVDKLLT GFDAPSLTYL YIDKKMQDHG LFQAVCRVNR LDSEDKDFGC IIDYSDLFDS
LQEAHSDYTN GAFENYERED IQGLISDKAQ KIKKKLEEVR GQLKSLGESV KEPKDEMDYI
AYFCGNDLEK NAQKRRLFYQ LVGAFLRMFV ELNNLEKPIY SKEETQKIKQ EAEFYRHLQK
AVGLSSGDSV DLKSYSEEMR RILDAYIKTT DSEVLFQIED QGLCEVLAQM DIDDFNKALS
QVFKNESSMA ESIANNTKKR IIEKEASDPK YYEKLSSLLN DLILQFREKK LTYLEYLQQI
HDLAKKVIDK EDRNYPKKIN TNALKILYDN LDENEALALE TDACIRDNKK DGWVGHNQKE
KNLKIALRKI INDEGLLENI FNLAKNIEEY R
//
