ID A0A133YUZ1_9FIRM Unreviewed; 337 AA.
AC A0A133YUZ1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=HMPREF3188_00616 {ECO:0000313|EMBL:KXB47010.1};
OS Tissierellia bacterium KA00581.
OC Bacteria; Bacillota; Tissierellia.
OX NCBI_TaxID=1588751 {ECO:0000313|EMBL:KXB47010.1, ECO:0000313|Proteomes:UP000070503};
RN [1] {ECO:0000313|EMBL:KXB47010.1, ECO:0000313|Proteomes:UP000070503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00581 {ECO:0000313|EMBL:KXB47010.1,
RC ECO:0000313|Proteomes:UP000070503};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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:KXB47010.1}.
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DR EMBL; LSCW01000040; KXB47010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133YUZ1; -.
DR STRING; 1588751.HMPREF3188_00616; -.
DR PATRIC; fig|1588751.3.peg.612; -.
DR OrthoDB; 9804478at2; -.
DR Proteomes; UP000070503; 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};
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:UP000070503}.
FT DOMAIN 56..187
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 6..186
FT /note="Large ATPase domain (RuvB-L)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT REGION 187..257
FT /note="Small ATPAse domain (RuvB-S)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT REGION 260..337
FT /note="Head domain (RuvB-H)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 26
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 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 133..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 296
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 315
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT BINDING 320
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
SQ SEQUENCE 337 AA; 37711 MW; A78B3E8F29F5FEB4 CRC64;
MFEEFEDRII GSGFSREDIE IETNLRPKWI DEYIGQEKAK ERLKIFIEAA KTRNEPLDHC
LLYGPPGLGK TTLANIIANE MGVNIRVTSG PAIEKPSDLA SILTNLSKDD VLFIDEIHRI
NRSVEEILYP AMEDYALDII IGKGPSARSL RIDLEKFTLI GATTRTGQLT GPLRDRFGIM
LNLELYSIEN LKKIITRSAG ILSVEIDEQG ALEIARRSRG TPRIANRLLK RVRDFAEVKK
DGKINLETAK AGLDILEVDS LGLDSIDRKI ILTIIDNFNG GPVGVDTIAA STGEERVTIE
DVYEPYLLQI GFLSRTSRGR IVTEKAYKHF GKIKNNN
//