ID   RUVB_COXBU              Reviewed;         351 AA.
AC   Q83BE0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
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};
GN   Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016};
GN   OrderedLocusNames=CBU_1570;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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   -!- 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   -!- 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; AE016828; AAO91067.1; -; Genomic_DNA.
DR   RefSeq; NP_820553.1; NC_002971.3.
DR   RefSeq; WP_005772105.1; NZ_CDBG01000001.1.
DR   AlphaFoldDB; Q83BE0; -.
DR   SMR; Q83BE0; -.
DR   STRING; 227377.CBU_1570; -.
DR   EnsemblBacteria; AAO91067; AAO91067; CBU_1570.
DR   GeneID; 1209480; -.
DR   KEGG; cbu:CBU_1570; -.
DR   PATRIC; fig|227377.7.peg.1571; -.
DR   eggNOG; COG2255; Bacteria.
DR   HOGENOM; CLU_055599_1_0_6; -.
DR   OrthoDB; 9804478at2; -.
DR   Proteomes; UP000002671; Chromosome.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Holliday junction branch migration complex subunit
FT                   RuvB"
FT                   /id="PRO_0000165525"
FT   REGION          1..186
FT                   /note="Large ATPase domain (RuvB-L)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   REGION          187..257
FT                   /note="Small ATPAse domain (RuvB-S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   REGION          260..351
FT                   /note="Head domain (RuvB-H)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         133..135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         296
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         315
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   BINDING         320
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   351 AA;  39151 MW;  7A69DB0B71CC72FF CRC64;
     MDEKIETRLI GATVQSNEPD LERSIRPKRL SDYIGQAAVR EQMDIFIRAA TNRREALDHV
     LIFGPPGLGK TTLAHIIAHE MQAGLKQTSG PVLEKAGDLA ALLTNLEPHD VLFIDEIHRL
     NPAIEEVLYP ALEDFQLDII IGEGPSARSI KLDLPPFTLV GATTRAGLLT SPLRDRFGIV
     QRLEFYRIPD LIHIVKRAAH ILNVVIDENG AGEIARRSRG TPRIANRLLR RVRDFAEVRA
     NGMINESIAK EALDLLNVDI RGLDVMDRKL LETIIKKFQG GPVGIESLAA AISEERGTIE
     DVIEPYLIQE GFILRTPRGR IATELTYQHF KLPLPTQSTL QENFDLLGKV E
//