ID   HSDR_STAS1              Reviewed;         930 AA.
AC   Q4A127;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Type I restriction enzyme SsaAORF53P endonuclease subunit {ECO:0000303|PubMed:12654995};
DE            Short=R protein;
DE            Short=SsaAORF53P {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:0000305}; OrderedLocusNames=SSP0054;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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 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,
CC       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; AP008934; BAE17199.1; -; Genomic_DNA.
DR   RefSeq; WP_002511775.1; NZ_MTGA01000037.1.
DR   AlphaFoldDB; Q4A127; -.
DR   SMR; Q4A127; -.
DR   STRING; 342451.SSP0054; -.
DR   REBASE; 11264; SsaAORF53P.
DR   EnsemblBacteria; BAE17199; BAE17199; SSP0054.
DR   KEGG; ssp:SSP0054; -.
DR   PATRIC; fig|342451.11.peg.54; -.
DR   eggNOG; COG0610; Bacteria.
DR   HOGENOM; CLU_004848_1_0_9; -.
DR   OMA; FTMNWAK; -.
DR   OrthoDB; 25184at2; -.
DR   PRO; PR:Q4A127; -.
DR   Proteomes; UP000006371; 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; Reference proteome; Restriction system.
FT   CHAIN           1..930
FT                   /note="Type I restriction enzyme SsaAORF53P endonuclease
FT                   subunit"
FT                   /id="PRO_0000077272"
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;  108873 MW;  559FA69A2AC96E24 CRC64;
     MVYQSEFALE TEMMEQLKSN GYETVTIRNE QQLLDNFRSI LNERHADKLN GDPLTDKEFQ
     RLLTMINGKG IFESARILRD KMPLKRDDES EVYLSFLDTR HWCQNKFQIT NQVSVDDTYK
     ARYDVTILIN GLPLVQIELK RRGIDINEAF NQVMRYRKQN YTGLFRYIQL FIISNGIDTR
     YISNNDGEIY KSHMFYWSDK ENNRINTLNE FTETFLRPCH IAKMISRYMI LNETDNILMA
     MRPYQVHAVE ALIHQATETS NNGYIWHTTG SGKTLTSFKA SQVLSEQDDI KKVIFLVDRK
     DLDSQTEEEF NKFSKGSVDK TNNTAQLVKQ LKDKSLPLIV TTIQKMSKAI QNNAEALDQY
     KTDKVVFIID ECHRSQFGDM HRIVRQHFNN AQYFGFTGTP RFEENQSQDG RSTADIFGRC
     LHTYLIKDAI HDGNVLGFSV DYINTIKAQN IDTETDELVE GINTDEVWLS DQRVELIARH
     ITENHDKYTR NRQYSAIFTV QSIPALVKYY DAFKKISKDY EHPLKVAGVF SYAANEERNE
     GEVDEAHSRG KLEEVIQDYN LNFGTNFSTD TFQEYFNHIS KNVKKGVKDN KIDVLIVVNM
     FLTGFDSKVL NTLYVDKNLK YHDLIQAYSR TNRVEKETKP FGKIVNYRDL KQNTDNALKL
     FSQTEDTDRV LMRDYDEYKA EFVDALAELK AVALKPQDMD QVQDENEKKA FVEAFRLVSK
     LVLRLKAFDE FDFTKANIGM NEQEFEDYKS KYFAIYDEVK PKRGEVEKVS ILNDIDFEIE
     ILRNDRINVS YIMDLVRQID LKDKAEQQRN RDQIRRMLDN ADDPTLRLKR DLLREFIDDV
     IPELSEEDNI DEAYILFENA KRESEFNQFA QQQAVDEQVL KDITGEYEYS GIVNQDHLKE
     LVGDKKLREK RQTKKAVTSF VEEVSEKYSS