ID   X2HC05_9NEIS            Unreviewed;      1020 AA.
AC   X2HC05;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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};
GN   ORFNames=SALWKB2_1200 {ECO:0000313|EMBL:AHN28582.1};
OS   Snodgrassella alvi wkB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Snodgrassella.
OX   NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN28582.1, ECO:0000313|Proteomes:UP000019668};
RN   [1] {ECO:0000313|EMBL:AHN28582.1, ECO:0000313|Proteomes:UP000019668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WkB2 {ECO:0000313|EMBL:AHN28582.1};
RX   PubMed=25053814;
RA   Kwong W.K., Engel P., Koch H., Moran N.A.;
RT   "Genomics and host specialization of honey bee and bumble bee gut
RT   symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
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|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC       ECO:0000256|RuleBase:RU364115}.
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DR   EMBL; CP007446; AHN28582.1; -; Genomic_DNA.
DR   RefSeq; WP_025330789.1; NZ_CP091515.1.
DR   AlphaFoldDB; X2HC05; -.
DR   STRING; 1196094.SALWKB2_1200; -.
DR   REBASE; 84404; SalwkB2ORF1197P.
DR   GeneID; 32536822; -.
DR   KEGG; salv:SALWKB2_1200; -.
DR   PATRIC; fig|1196094.4.peg.1201; -.
DR   HOGENOM; CLU_005762_0_0_4; -.
DR   OrthoDB; 9758243at2; -.
DR   Proteomes; UP000019668; 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   CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR   CDD; cd22332; HsdR_N; 1.
DR   CDD; cd18800; SF2_C_EcoR124I-like; 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:SF15; TYPE I RESTRICTION ENYME HINDI 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          287..453
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   1020 AA;  116238 MW;  91FEBAA2F5995F63 CRC64;
     MFNEQTVTEN GIISRLKELS GINWSYCHGE SLPKQSRDIF VDEWLKDALC SLNPDIAKQP
     DYADEVIYKL RGVILEAAHT GLVKANENFY EWLMAEKTLP FGENGDHITI NLIDFDNIDN
     NHFVVSQQVH YIAATEVYFD IVLYVNGIPL VVGEVKTATR PSVTWQDGAA DFMGGKKHYW
     KNIEPFFVPN LLCFASEGKT FAYGAINARV KDWGPWHSTE LRDEILPGLA SVLNSCEGLL
     NPQTLLQLLE SFALFSTVKT GKNTPPKRIK LLPRYPQFEA AKQIVERVRK GYPKKGLIWH
     FQGSGKSLLM LYAAKMLRAD NALKNPTVLV VVDRRDLDSQ INETFGGADV KNLIKVQSCK
     KLGEYIEQDS RGILITTIFK FKDVEIDDSN PNGLNSRDNI IVLVDEAHRT QEGGLGEKMR
     WALPNAHFYG LTGTPISGID RNTFKLFGAD EDPGRYMNRY SYKQSIRDGS TNPVKFEPRL
     AELRVDRDAI NEEFKQLVKE NDLDDEEKAA LSKRAGKLAI MLKAPKRMTA ISSDIAKHFT
     SHVKPKKMKG MVVVYDREAC VQMYYLLGEK LGFDAIEVVM NVDQAPIKAK EGDKKDKVNN
     DWRKWHDELK LPIKQEDFER WQNIDAESQV QKELIECYKD PKHPLQLIIV TAKLLTGFDA
     PICYCMYLDK PLRDHTLLQA MCRTNRLYET DDTRKDMGLI IDYLGVFENL RTALAYKPEE
     IDGVVEGIEA FKKLLPAQLD KCLSFFPNVD RTLEGFEGIM AAQECLPTNK KRDEFAACFG
     VLSKLWSAIS PDPFLSPYRQ NYKWLAQIYE SVRPVGQTGA LVWAALGPET IKMIHEHTDI
     NRIRDDIDEL IMDEHAIFTL TEKEQEQRAK RLEIDLMGRL RGSHEPKFVE LGERLEKLRQ
     DYEAGVIKAI EWLKGLLDAA KDTVQAERET GEHPVTEADN KQALTKLFLE TRPESTPKLI
     GDVVEQIDKI VKATRFDGWQ NSNSGPREIQ KALLLTLAQF GLGKDMELFQ KAYGYIEEHY
//