ID O68167_9LACT Unreviewed; 995 AA.
AC O68167;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 91.
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};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN Name=hsdR {ECO:0000313|EMBL:AAC38345.1};
OS Lactococcus lactis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1358 {ECO:0000313|EMBL:AAC38345.1};
RN [1] {ECO:0000313|EMBL:AAC38345.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL1403 {ECO:0000313|EMBL:AAC38345.1};
RX PubMed=9593305; DOI=10.1046/j.1365-2958.1998.00787.x;
RA Schouler C., Gautier M., Ehrlich S.D., Chopin M.C.;
RT "Combinational variation of restriction modification specificities in
RT Lactococcus lactis.";
RL Mol. Microbiol. 28:169-178(1998).
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|ARBA:ARBA00011296,
CC 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; AF013165; AAC38345.1; -; Genomic_DNA.
DR AlphaFoldDB; O68167; -.
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; cd22332; HsdR_N; 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:SF16; TYPE I RESTRICTION ENZYME 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 278..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 995 AA; 113590 MW; F9628A26995AFA86 CRC64;
MAEAKFEAAL IKKLEAEGWT YRKDLSYVSI KVLEGHWREV LNENNAYKLN GKPLSDVEFG
LVMQEVQRIK TPYDAQLLLV GAGGVGSIPI TRDDGSNLEV EIFYEDDVAG GRSRYEVVSQ
VIFDELPHGL ASKRIIDLAL LINGIPVAHI EEKDEHLQNQ WGAFEQLKGY HGEGLYEGLF
AFVQVQFILS QHSANYFARP NRLENYNKTF VFGWRDEQQK DITDAFVFAH QVLGIPALHR
LVTVNMIPDA SNSNLMVMRS YQIQATRAIL QRMKEMEHND YIQKEGGYIW HTTGSGKTVT
SFKVAQLLAA APKVKNVLFI VDRVDLVDQT LENFKDFAYI QFKNRIKKVN GRELKRELSH
KGASQILLIS VQGLTKAVKN GLKNTDRNVI IMDEAHRSAN GESVQLIKSA FQKTTWFGFT
GTPNFYSDEI NDVQTTRDIS THDIFGKRLH SYTIKDAIGD GNVLGFDITY FNPTIEIESL
DEEHSEKDYE KEVYQSHVYR EQVVQDILNL WDKTSSGALV AGKREKNVFQ AMLAVSGKQA
VVHYYNLFKE KAPHLRVAMT FSRDESNQPG TKEQNEALKK AIKEYSSCFN VPSLLNAQEP
ARAYMIDITK RLARKKPYNQ GKDEDRLDLV IVSDQLLTGF DSKYINTIYM DKQLREGMLI
QAMSRTNRTF HLNSKPHGKV RFYRQGEQMK SFVENALRIY SRGGNDTLQG ADEDSKNEDI
QSLEDEHILA EPQSHQIPKL TPAVQELKAF AGEDFSQIPR GEKDLKQFVR LGLETQNQIQ
QLVQQGYELG NEIDLLDAQG ESTGEKVRLD ISSFEEFGAL QARLNDAREK LPEEERPDLT
EIRVGLSLYD HEIIDYDWLV DLLNLFMDQK TPENKASIEK HILPLDEMSQ QEIKDIIVDI
ESGEIKEHFT KATLEDQRKH KRSDRQELKI RRWAANQKVN GNRIVQAFDL FLPGHSLVDN
SQLSALVSEI EAEENLSFFG ASEFETALMS FFNSL
//
