ID   HSDR_STAEQ              Reviewed;         930 AA.
AC   Q5HK76;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Type I restriction enzyme SepRPIP endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            Short=SepRPIP {ECO:0000303|PubMed:12654995};
DE            EC=3.1.21.3 {ECO:0000250|UniProtKB:P08956};
DE   AltName: Full=Type-1 restriction enzyme endonuclease subunit;
GN   Name=hsdR {ECO:0000303|PubMed:15774886}; OrderedLocusNames=SERP2474;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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 may recognize 5'-GAGN(7)TAC-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; CP000029; AAW53360.1; -; Genomic_DNA.
DR   RefSeq; WP_002489617.1; NC_002976.3.
DR   AlphaFoldDB; Q5HK76; -.
DR   SMR; Q5HK76; -.
DR   STRING; 176279.SERP2474; -.
DR   REBASE; 10764; SepRPIP.
DR   REBASE; 182831; Bli37IP.
DR   REBASE; 233047; SpaF3KORF1139P.
DR   EnsemblBacteria; AAW53360; AAW53360; SERP2474.
DR   KEGG; ser:SERP2474; -.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_004848_1_0_9; -.
DR   OMA; FTMNWAK; -.
DR   OrthoDB; 25184at2; -.
DR   PRO; PR:Q5HK76; -.
DR   Proteomes; UP000000531; 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; 2.
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; Reference proteome; Restriction system.
FT   CHAIN           1..930
FT                   /note="Type I restriction enzyme SepRPIP endonuclease
FT                   subunit"
FT                   /id="PRO_0000077271"
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   930 AA;  109659 MW;  AFE422D1D08A0A1D CRC64;
     MVYQSEYALE NEVLQQLENL GYERVNIHNV EQLHDNFRTI INERHKEKLN GKPLTDREFE
     RLMTGINGKS VFDSAMQLRD SYVLKRDDDT DLYLNFMNLK QWCQNKFQVT NQISVKDKYK
     SRYDVTILIN GLPLVQIELK RSGVAITEAF NQIERYRRQN YTGLFRYIQL FVVSNKMETR
     YYANSDREIF KGQMFYWSNE QNERINYLKD FIEDFLESCH ISKMISRYMV VNETDKFLMA
     LRPYQVYAVE AILNRALETN NNGYIWHTTG SGKTLTSFKA SQLLSQEENI KKVIFLVDRK
     DLDNQTLAEF NKFQEDSVDF TDNTRKLLKQ LADPTLPLIV TTIQKMANAV KSNHSVMESY
     KQDKVIFIID ECHRTQFGDM HRLIKQHFEN AQYFGFTGTP RFEENKSQDG RATADIFDKC
     LHHYLIKDAI RDHNVLGFSV EYNQTFNSHE DLDEEYISKI NTSEIWMADE RIEAVCRHLI
     SNYHKKTDNG NYTSMFAVQS IPMAIKYYDT FQRLKNEGVH DLNVATIFTY QANEDAQEDE
     NHVHSREVLD RIMNDYNQTF KTNYNTDNFE GYFSDVSKRM KEVVRDDKID ILIVVNMFLT
     GFDSKKLNTL YVDKNLKHHD LIQAYSRTNR VEKERKPYGN IVCYRDLKKQ TDEAIEIFSQ
     TDNTDTVLSL SYEEYLDNFK DILQDVFQLA PTPLDVDKLE AEDLKKEFVI SFRDLSNTLI
     KLKTFDEFQF TEDELGIAEQ TYEDYKGKYL NIYEEVMRGK KVDGEEGVSV LDDIDFQVEL
     MRNDLINVKY IMDLIGQINL SDAKARDEKR HQIHKLLDKA DDQQLRLKAD LIRSFLDKVV
     PSLKEDSDIN EAYYEFEDKE KTKEIDAFAE QKAFSAMLLN EAVNEYEYSG NIDRKSIGQN
     ISEPFMKRKR KTDQIIQFIE DTVEKYGVVE