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Entry: A0A1G2PE90_9BACT
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ID   A0A1G2PE90_9BACT        Unreviewed;       346 AA.
AC   A0A1G2PE90;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-NOV-2023, entry version 23.
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=A2828_01995 {ECO:0000313|EMBL:OHA46654.1};
OS   Candidatus Terrybacteria bacterium RIFCSPHIGHO2_01_FULL_43_35.
OC   Bacteria; Candidatus Terrybacteria.
OX   NCBI_TaxID=1802361 {ECO:0000313|EMBL:OHA46654.1, ECO:0000313|Proteomes:UP000178869};
RN   [1] {ECO:0000313|EMBL:OHA46654.1, ECO:0000313|Proteomes:UP000178869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHA46654.1}.
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DR   EMBL; MHSR01000013; OHA46654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2PE90; -.
DR   Proteomes; UP000178869; 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:OHA46654.1};
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          183..253
FT                   /note="Small ATPAse domain (RuvB-S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00016"
FT   REGION          256..346
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         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   346 AA;  38257 MW;  F940497CB2CB20A4 CRC64;
     MPLPPDGQPV EKEEDFLAQT LRPQTFVEYI GQQKTKDNLS VAIGAAQIRR EPLEHVLIHG
     PAGIGKTTLA YLIAKEMRSS LRVTSGPAIE KVGDLAAILT NLEAGDVLFI DEVHRLSKLI
     EEILYPAMES RSLDIVLGKG GGARTIQLPL PPFTLIAATT RIGLLSSPLR SRFGSTFRLE
     FYSEQEIEEI LNRSAKILGV SLTPEASKKL AVSSRSTPRV ANRLLKRCRD LAQVEKHNII
     DEQIVSRALK MLEIDEVGLE SSDRKILRVL IEHFNGGPAG IQAIAASSSE EEETILEVFE
     PYLLRIGFLT RTPRGRAATK AAYRHLGVNF PKKIDDARDH NNESML
//
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