ID   RUVB_SHESR              Reviewed;         334 AA.
AC   Q0HUZ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Shewmr7_2076;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI43064.1; -; Genomic_DNA.
DR   RefSeq; WP_011626231.1; NC_008322.1.
DR   AlphaFoldDB; Q0HUZ1; -.
DR   SMR; Q0HUZ1; -.
DR   EnsemblBacteria; ABI43064; ABI43064; Shewmr7_2076.
DR   KEGG; shm:Shewmr7_2076; -.
DR   HOGENOM; CLU_055599_1_0_6; -.
DR   OMA; IHRMSRP; -.
DR   OrthoDB; 874197at2; -.
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..334
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT                   /id="PRO_1000001478"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   334 AA;  36855 MW;  85D84F7B9E588E5C CRC64;
     MIEADRLIQP QLQGQDDVID RAMRPKLLDE YTGQDDTRAQ LKVFIQAAKN REEALDHMLI
     YGPPGLGKTT LAMIVANEMG VNIKSTSGPV LEKAGDLAAL LTNLEAGDVL FIDEIHRLSP
     VVEEILYPAM EDYQLDIMIG EGPAARSIKL DLPPFTLVGA TTRAGALTSP LRARFGIPLR
     LEFYNVKDLS TIVSRSAQVM GLAIDSEGAI EIAKRSRGTP RIANRLLRRV RDYAEVKHDG
     AVTKKVAEHA LDLLDVDGEG FDYMDRKLLL AIIDKFMGGP VGLDNLAAAI GEERETIEDV
     LEPFLIQQGF IQRTPRGRIA TNRAYLHFGM IKPE