ID A0A089JG28_9BACL Unreviewed; 335 AA.
AC A0A089JG28;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=H70357_27520 {ECO:0000313|EMBL:AIQ20044.1};
OS Paenibacillus sp. FSL H7-0357.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ20044.1, ECO:0000313|Proteomes:UP000029508};
RN [1] {ECO:0000313|EMBL:AIQ20044.1, ECO:0000313|Proteomes:UP000029508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ20044.1,
RC ECO:0000313|Proteomes:UP000029508};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009241; AIQ20044.1; -; Genomic_DNA.
DR RefSeq; WP_038595609.1; NZ_CP009241.1.
DR AlphaFoldDB; A0A089JG28; -.
DR STRING; 1536774.H70357_27520; -.
DR KEGG; paeh:H70357_27520; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_9; -.
DR Proteomes; UP000029508; 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 {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:AIQ20044.1};
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}.
FT DOMAIN 52..183
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 2..182
FT /note="Large ATPase domain (RuvB-L)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT REGION 183..253
FT /note="Small ATPAse domain (RuvB-S)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT REGION 256..335
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 335 AA; 36991 MW; 1869C93E79860475 CRC64;
MDDRIISANL MMDEQAVELS LRPRYLGEYI GQTQVKENLK IYIEAAKMRS EALDHVLLYG
PPGLGKTTLA NIIANELGVN LRTTSGPAIE RPGDLAALLT NLQEGDVLFI DEIHRLHRTV
EEVMYPAMED FALDIMIGKG PSARSVRLDL PPFTLIGATT RAGLLSAPLR DRFGVVSRLE
YYTIDELSFI VSRNAELLGI EILGDAAEEI ALRARGTPRI ANRLLKRVRD FAQVRGDGII
TPDIAGESLK MLQVDPRGLD SIDHKMLHSM ITAFRGGPVG LDTIAATIGE ESQTIEDVYE
PYLLQIGFLQ RTPRGRVVTP AAYHHLGLPL PPEQH
//
