ID   RUVB_THETH              Reviewed;         324 AA.
AC   Q56214; Q9RA64;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-NOV-2023, entry version 112.
DE   RecName: Full=Holliday junction branch migration complex subunit RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:8626340};
GN   Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016,
GN   ECO:0000303|PubMed:8626340};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND DNA-BINDING.
RX   PubMed=8626340; DOI=10.1128/jb.178.9.2695-2700.1996;
RA   Tong J., Wetmur J.G.;
RT   "Cloning, sequencing, and expression of ruvB and characterization of RuvB
RT   proteins from two distantly related thermophilic eubacteria.";
RL   J. Bacteriol. 178:2695-2700(1996).
CC   -!- FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ)
CC       DNA during genetic recombination and DNA repair, while the RuvA-RuvB
CC       complex plays an important role in the rescue of blocked DNA
CC       replication forks via replication fork reversal (RFR). RuvA
CC       specifically binds to HJ cruciform DNA, conferring on it an open
CC       structure. The RuvB hexamer acts as an ATP-dependent pump, pulling
CC       dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on
CC       either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per
CC       hexamer contact DNA at a time. Coordinated motions by a converter
CC       formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and
CC       nucleotide exchange. Immobilization of the converter enables RuvB to
CC       convert the ATP-contained energy into a lever motion, pulling 2
CC       nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus
CC       driving DNA branch migration. The RuvB motors rotate together with the
CC       DNA substrate, which together with the progressing nucleotide cycle
CC       form the mechanistic basis for DNA recombination by continuous HJ
CC       branch migration. Branch migration allows RuvC to scan DNA until it
CC       finds its consensus sequence, where it cleaves and resolves cruciform
CC       DNA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- FUNCTION: Has Mg(2+)-, DNA-dependent ATPase activity; dsDNA and
CC       supercoiled DNA but not ssDNA stimulate activity. Binds to linear dsDNA
CC       in the absence of ATP or ATP-gamma-S. This subunit can promote Holliday
CC       junction migration alone in vitro. Partially complements an E.coli
CC       deletion for UV sensitivity. {ECO:0000269|PubMed:8626340}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00016,
CC         ECO:0000269|PubMed:8626340};
CC   -!- ACTIVITY REGULATION: The ATPase activity of RuvB is enhanced by RuvA.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature for ATPase activity is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:8626340};
CC   -!- SUBUNIT: Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ)
CC       complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters
CC       through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA
CC       strand where it exits the tetramer. Each RuvB hexamer is contacted by
CC       two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this
CC       complex drives branch migration. In the full resolvosome a probable
CC       DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
CC       {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- DOMAIN: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S)
CC       domains and the C-terminal head (RuvB-H) domain. The head domain binds
CC       DNA, while the ATPase domains jointly bind ATP, ADP or are empty
CC       depending on the state of the subunit in the translocation cycle.
CC       During a single DNA translocation step the structure of each domain
CC       remains the same, but their relative positions change.
CC       {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00016}.
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DR   EMBL; U22817; AAB03726.2; -; Genomic_DNA.
DR   PIR; T11851; T11851.
DR   AlphaFoldDB; Q56214; -.
DR   SMR; Q56214; -.
DR   DIP; DIP-41108N; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_00016; DNA_HJ_migration_RuvB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041445; AAA_lid_4.
DR   InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008824; RuvB-like_N.
DR   InterPro; IPR008823; RuvB_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00635; ruvB; 1.
DR   PANTHER; PTHR42848; -; 1.
DR   PANTHER; PTHR42848:SF1; HOLLIDAY JUNCTION ATP-DEPENDENT DNA HELICASE RUVB; 1.
DR   Pfam; PF17864; AAA_lid_4; 1.
DR   Pfam; PF05491; RuvB_C; 1.
DR   Pfam; PF05496; RuvB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..324
FT                   /note="Holliday junction branch migration complex subunit
FT                   RuvB"
FT                   /id="PRO_0000165620"
FT   REGION          1..168
FT                   /note="Large ATPase domain (RuvB-L)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   REGION          169..239
FT                   /note="Small ATPAse domain (RuvB-S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   REGION          242..324
FT                   /note="Head domain (RuvB-H)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         6
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         7
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         115..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         297
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         302
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   324 AA;  36016 MW;  1B0DB92F373185CE CRC64;
     MEDLALRPKT LDEYIGQERL KQKLRVYLEA AKARKEPLEH LLLFGPPGLG KTTLAHVIAH
     ELGVNLRVTS GPAIEKPGDL AAILANSLEE GDILFIDEIH RLSRQAEEHL YPAMEDFVMD
     IVIGQGPAAR TIRLELPRFA LIGATTRPGL ITAPLLSRFG IVEHLEYYTP EELAQGVMRD
     ARLLGVRITE EAALEIGRRS RGTMRVAKRL FRRVRDFAQV EGEEVITRER ALEALAALGL
     DELGLEKRDR EILEVLILRF GAGPVGLATL ATALSEDPGT LEEVHEPYLI RQGLLKRTPR
     GRVATELAYR HLGYPPPVGP LLEP
//