ID   RUVB_BURM9              Reviewed;         356 AA.
AC   A2S594;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Holliday junction ATP-dependent DNA helicase 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=BMA10229_A1128;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC       cruciform structure in supercoiled DNA with palindromic sequence,
CC       indicating that it may promote strand exchange reactions in homologous
CC       recombination. RuvAB is a helicase that mediates the Holliday junction
CC       migration by localized denaturation and reannealing.
CC       {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: Forms a complex with RuvA. {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; CP000546; ABN02350.1; -; Genomic_DNA.
DR   RefSeq; WP_004194268.1; NC_008836.1.
DR   AlphaFoldDB; A2S594; -.
DR   SMR; A2S594; -.
DR   EnsemblBacteria; ABN02350; ABN02350; BMA10229_A1128.
DR   GeneID; 56593683; -.
DR   KEGG; bml:BMA10229_A1128; -.
DR   HOGENOM; CLU_055599_1_0_4; -.
DR   OMA; IHRMSRP; -.
DR   Proteomes; UP000002283; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00016; DNA_helic_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   PANTHER; PTHR42848; PTHR42848; 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; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00635; ruvB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; Helicase;
KW   Hydrolase; Nucleotide-binding; SOS response.
FT   CHAIN           1..356
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT                   /id="PRO_1000001372"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   356 AA;  39223 MW;  3931D5D7708C924D CRC64;
     MIETDKLAAE RIIAATPASS HEEAFERALR PRQLDEYVGQ EKVRDQLEIF IEAAKRRSEA
     LDHVLLFGPP GLGKTTLAHI IAREMGVNLR QTSGPVLERA GDLAALLTNL EANDVLFIDE
     IHRLSPVVEE ILYPALEDYQ IDIMIGEGPA ARSVKLDLQP FTLVGATTRA GMLTNPLRDR
     FGIVARLEFY DAEQLSRIVR RSAALLNAQI DPAGALEIAK RSRGTPRIAN RLLRRVRDYA
     EVKADGNITA AVADAALAML DVDPVGFDLM DRKLLEAILH KFDGGPVGVD NLAAAIGEER
     DTIEDVLEPY LIQQGFLQRT PRGRVATLLT YRHFGLSAPD AANPVRNLWD TPDAEC