ID   HSDR_STAAN              Reviewed;         929 AA.
AC   Q7A801;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Type I restriction enzyme SauN315I endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            Short=SauN315I {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 {ECO:0000303|PubMed:11418146}; OrderedLocusNames=SA0189;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: The restriction (R) subunit of a type I restriction enzyme
CC       that may recognize 5'-AGGN(5)GAT-3' and cleaves a random distance away.
CC       Subunit R is required for both nuclease and ATPase activities, but not
CC       for modification. After locating a non-methylated recognition site, the
CC       enzyme complex serves as a molecular motor that translocates DNA in an
CC       ATP-dependent manner until a collision occurs that triggers cleavage.
CC       {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; BA000018; BAB41410.1; -; Genomic_DNA.
DR   PIR; G89781; G89781.
DR   RefSeq; WP_000331330.1; NC_002745.2.
DR   AlphaFoldDB; Q7A801; -.
DR   SMR; Q7A801; -.
DR   REBASE; 392165; Eco6193ORF3821P.
DR   REBASE; 5117; SauN315I.
DR   EnsemblBacteria; BAB41410; BAB41410; BAB41410.
DR   KEGG; sau:SA0189; -.
DR   HOGENOM; CLU_004848_1_0_9; -.
DR   OMA; FTMNWAK; -.
DR   PRO; PR:Q7A801; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Restriction system.
FT   CHAIN           1..929
FT                   /note="Type I restriction enzyme SauN315I endonuclease
FT                   subunit"
FT                   /id="PRO_0000077267"
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;  109294 MW;  7814981B5A925187 CRC64;
     MAYQSEYALE NEMMNQLEQL GYERVTIRDN KQLLDNFRTI LNERHADKLE GNPLTDKEFQ
     RLLTMIDGKS IFESARILRD KLPLRRDDES EIYLSFLDKK 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 EQPLTIAGIF TFKPNEDDRD
     GEVPYHSREK LEIMISDYNK KFETNFSTDT TNEYFNHISK NVKKGVKDSK IDILIVVNMF
     LTGFDSKVLN TLYVDKNLMY HDLIQAYSRT NRVEKESKPF GKIVNYRDLK KETDDALRVF
     SQTNDTDTIL MRSYEEYKKE FMDAYRELKM IVPTPHMVDD IQDEEELKRF VEAYRLLAKI
     ILRLKAFDEF EFTIDEIGMD EQENEDYKSK YLAVYDQVKR ATAEKNKVSI LNDIDFEIEM
     MRNDTINVNY IMNILRQIDL EDKAEQRRNQ EQIRRILDHA DDPTLRLKRD LIREFIDNVV
     PSLNKDDDID QEYVNFESIK KEAEFKGFAG ERSIDEQALK TISNDYQYSG VVNPHHLKKM
     IGDLPLKEKR KARKAIESFV AETTEKYGV