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Entry: A0A369BAB6_9FIRM
LinkDB: A0A369BAB6_9FIRM
Original site: A0A369BAB6_9FIRM 
ID   A0A369BAB6_9FIRM        Unreviewed;       331 AA.
AC   A0A369BAB6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Holliday junction branch migration complex subunit RuvB {ECO:0000256|HAMAP-Rule:MF_00016};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_00016};
GN   Name=ruvB {ECO:0000256|HAMAP-Rule:MF_00016};
GN   ORFNames=DFR58_10751 {ECO:0000313|EMBL:RCX17506.1};
OS   Anaerobacterium chartisolvens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerobacterium.
OX   NCBI_TaxID=1297424 {ECO:0000313|EMBL:RCX17506.1, ECO:0000313|Proteomes:UP000253034};
RN   [1] {ECO:0000313|EMBL:RCX17506.1, ECO:0000313|Proteomes:UP000253034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27016 {ECO:0000313|EMBL:RCX17506.1,
RC   ECO:0000313|Proteomes:UP000253034};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001665, ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-Rule:MF_00016}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00016}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00016}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00016}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCX17506.1}.
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DR   EMBL; QPJT01000007; RCX17506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369BAB6; -.
DR   OrthoDB; 9804478at2; -.
DR   Proteomes; UP000253034; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00016};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00016};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00016}; Helicase {ECO:0000313|EMBL:RCX17506.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00016};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00016}; Reference proteome {ECO:0000313|Proteomes:UP000253034}.
FT   DOMAIN          52..179
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          183..253
FT                   /note="Small ATPAse domain (RuvB-S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   REGION          256..331
FT                   /note="Head domain (RuvB-H)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         129..131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         311
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   BINDING         316
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
SQ   SEQUENCE   331 AA;  36795 MW;  A8D3187570DEDC7A CRC64;
     MEEERLVGCE VKQEDRDEFS LRPRKLSDYV GQAKVKENLT VFIEAARRRN EALDHVLLYG
     PPGLGKTTLA SIIASELGVN IRITSGPAIE KPGDLAAILT NLGNYDVLFI DEIHRLNRSV
     EEILYPAMED YALDIIIGKG PSARSIRLDL PKFTLIGATT RAGLLTAPLR DRFGVINRLE
     MYSPQELKLI VKRSAGILGI EIDEEGADEI SGRSRGTPRI SNRLLKRVRD FAQVRAEGYI
     TKEVARMSLN ALEIDPIGLD GVDRNMLMSI IDKFAGGPVG LETLAASIGE ETETIEDVYE
     PYLLQLGFIN KTPRGRIATK LAYEHFGLRY E
//
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