ID   HSDR_STAAR              Reviewed;         929 AA.
AC   Q6GKB1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Type I restriction enzyme SauMRSORF196P endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            Short=SauMRSORF196P {ECO:0000303|PubMed:12654995};
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
DE   AltName: Full=Type-1 restriction enzyme R protein;
GN   Name=hsdR; OrderedLocusNames=SAR0196;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN   [2]
RP   NOMENCLATURE.
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 restriction (R) subunit of a type I restriction enzyme
CC       that recognizes an undetermined sequence and cleaves a random distance
CC       away. Subunit R is required for both nuclease and ATPase activities,
CC       but not for modification. After locating a non-methylated recognition
CC       site, the enzyme complex serves as a molecular motor that translocates
CC       DNA in an ATP-dependent manner until a collision occurs that triggers
CC       cleavage. {ECO:0000250|UniProtKB:P08956, ECO:0000303|PubMed:12654995}.
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. {ECO:0000250|UniProtKB:P08956}.
CC   -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC       multifunctional systems which require ATP, S-adenosyl methionine and
CC       magnesium as cofactors and, in addition to their endonucleolytic and
CC       methylase activities, are potent DNA-dependent ATPases.
CC       {ECO:0000250|UniProtKB:P08956}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG39223.1; -; Genomic_DNA.
DR   RefSeq; WP_000331344.1; NC_002952.2.
DR   AlphaFoldDB; Q6GKB1; -.
DR   SMR; Q6GKB1; -.
DR   REBASE; 9403; SauMRSORF196P.
DR   KEGG; sar:SAR0196; -.
DR   HOGENOM; CLU_004848_1_0_9; -.
DR   OMA; FTMNWAK; -.
DR   OrthoDB; 25184at2; -.
DR   PRO; PR:Q6GKB1; -.
DR   Proteomes; UP000000596; 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   Gene3D; 3.40.50.300; -; 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   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; SSF52540; 1.
DR   TIGRFAMs; TIGR00348; hsdR; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Restriction system.
FT   CHAIN           1..929
FT                   /note="Type I restriction enzyme SauMRSORF196P endonuclease
FT                   subunit"
FT                   /id="PRO_0000077268"
FT   DOMAIN          254..418
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         268..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   929 AA;  109235 MW;  4D35FF94AA43AB57 CRC64;
     MAYQSEYALE NEMMNQLEQL GYERVTIRDN KQLLDNFRTI LNERHADKLE GNPLTDKEFQ
     RLLTMIDGKS IFESARILRD KLPLRRDDES EIYLSFLDTK SWCKNKFQVT NQVSVEDTYK
     ARYDVTILIN GLPLVQVELK RRGIDINEAF NQVKRYRKQN YTGLFRYIQM FIISNGVETR
     YFSNNDSELL KSHMFYWSDK QNNRINTLQS FAESFMRPCQ LAKMISRYMI INETDRILMA
     MRPYQVYAVE ALIQQATETG NNGYVWHTTG SGKTLTSFKA SQILSQQDDI KKVIFLVDRK
     DLDSQTEEEF NKFAKGAVDK TFNTSQLVRQ LNDKSLPLIV TTIQKMAKAI QGNAHLLEQY
     KTNKVVFIID ECHRSQFGDM HRLVKQHFKN AQYFGFTGTP RFPENSSQDG RTTADIFGRC
     LHTYLIRDAI HDGNVLGFSV DYINTFKNKA LKAEDNSMVE AIDTEEVWLA DKRVELVTRH
     IINNHDKYTR NRQYSSIFTV QSIHALIKYY ETFKRLNKKL EQPLTVAGIF TFKPNEDDRD
     GEVPYHSREK LEIMISDYNK KFETNFSTDT TNEYFNHISK NVKKGVKDSK IDILIVVNMF
     LTGFDSKVLN TLYVDKNLMY HDLIQAYSRT NRVEKESKPF GKIVNYRDLK KETDDALRVF
     SQTNDTDTIL MRSYEEYKKE FIDAYRELKM IVPTPHMVDD IQDEEELKRF VEAYRLLAKI
     ILRLKAFDEF EFTIDEIGMD EQENEDYKSK YLAVYDQVKR ATAEKNKVSI LNDIDFEIEM
     MRNDTINVNY IMNILRQIDL EDKAEQRRNQ EQIRRILDHA DDPTLRLKRD LIREFIDNVV
     PSLNKDDDID QEYVNFESIK KEAEFKGFAG ERSIDEQALK TISNDYQYSG VVNPHHLKKM
     IGDLPLKEKR KARKAIESFV AETTEKYGV