ID RUVB_ECOLI Reviewed; 336 AA.
AC P0A812; P08577;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=Holliday junction branch migration complex subunit RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:8433990};
GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000303|PubMed:2842314,
GN ECO:0000303|PubMed:3279394}; OrderedLocusNames=b1860, JW1849;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1] {ECO:0000312|EMBL:CAA30120.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=K12;
RX PubMed=3279394; DOI=10.1093/nar/16.4.1541;
RA Benson F.E., Illing G.T., Sharples G.J., Lloyd R.G.;
RT "Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a
RT LexA regulated operon encoding two genes.";
RL Nucleic Acids Res. 16:1541-1549(1988).
RN [2] {ECO:0000312|EMBL:AAA24613.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND OPERON STRUCTURE.
RX PubMed=2842314; DOI=10.1128/jb.170.9.4322-4329.1988;
RA Shinagawa H., Makino K., Amemura M., Kimura S., Iwasaki H., Nakata A.;
RT "Structure and regulation of the Escherichia coli ruv operon involved in
RT DNA repair and recombination.";
RL J. Bacteriol. 170:4322-4329(1988).
RN [3] {ECO:0000312|EMBL:AAC74930.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4] {ECO:0000312|EMBL:AAC74930.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5] {ECO:0000312|EMBL:BAA15671.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION AS A WEAK ATPASE, ACTIVITY REGULATION,
RP SUBUNIT, AND NUCLEOTIDE-BINDING.
RX PubMed=2529252; DOI=10.1128/jb.171.10.5276-5280.1989;
RA Iwasaki H., Shiba T., Makino K., Nakata A., Shinagawa H.;
RT "Overproduction, purification, and ATPase activity of the Escherichia coli
RT RuvB protein involved in DNA repair.";
RL J. Bacteriol. 171:5276-5280(1989).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=6374379; DOI=10.1007/bf00383532;
RA Lloyd R.G., Benson F.E., Shurvinton C.E.;
RT "Effect of ruv mutations on recombination and DNA repair in Escherichia
RT coli K12.";
RL Mol. Gen. Genet. 194:303-309(1984).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=2693946; DOI=10.1007/bf00261196;
RA Iwasaki H., Shiba T., Nakata A., Shinagawa H.;
RT "Involvement in DNA repair of the ruvA gene of Escherichia coli.";
RL Mol. Gen. Genet. 219:328-331(1989).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AB1157;
RX PubMed=2164626; DOI=10.1007/bf00261724;
RA Sharples G.J., Benson F.E., Illing G.T., Lloyd R.G.;
RT "Molecular and functional analysis of the ruv region of Escherichia coli K-
RT 12 reveals three genes involved in DNA repair and recombination.";
RL Mol. Gen. Genet. 221:219-226(1990).
RN [10]
RP FUNCTION.
RX PubMed=1833759; DOI=10.1073/pnas.88.19.8445;
RA Shiba T., Iwasaki H., Nakata A., Shinagawa H.;
RT "SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli:
RT functional interactions between RuvA and RuvB for ATP hydrolysis and
RT renaturation of the cruciform structure in supercoiled DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8445-8449(1991).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1435721; DOI=10.1007/bf00286175;
RA Tsaneva I.R., Illing G., Lloyd R.G., West S.C.;
RT "Purification and properties of the RuvA and RuvB proteins of Escherichia
RT coli.";
RL Mol. Gen. Genet. 235:1-10(1992).
RN [12]
RP PROBABLE FUNCTION IN HOLLIDAY JUNCTION, AND COFACTOR.
RX PubMed=1608954; DOI=10.1073/pnas.89.12.5452;
RA Parsons C.A., Tsaneva I., Lloyd R.G., West S.C.;
RT "Interaction of Escherichia coli RuvA and RuvB proteins with synthetic
RT Holliday junctions.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5452-5456(1992).
RN [13]
RP FUNCTION, AND COFACTOR.
RX PubMed=1617728; DOI=10.1016/0092-8674(92)90638-s;
RA Tsaneva I.R., Mueller B., West S.C.;
RT "ATP-dependent branch migration of Holliday junctions promoted by the RuvA
RT and RuvB proteins of E. coli.";
RL Cell 69:1171-1180(1992).
RN [14]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=8393934; DOI=10.1006/jmbi.1993.1399;
RA Parsons C.A., West S.C.;
RT "Formation of a RuvAB-Holliday junction complex in vitro.";
RL J. Mol. Biol. 232:397-405(1993).
RN [15]
RP INCORRECT FUNCTION AS A HELICASE DIRECTIONALITY, AND CATALYTIC ACTIVITY.
RX PubMed=8433990; DOI=10.1073/pnas.90.4.1315;
RA Tsaneva I.R., Mueller B., West S.C.;
RT "RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity
RT in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1315-1319(1993).
RN [16]
RP SUBUNIT, AND DNA-BINDING.
RX PubMed=8052630; DOI=10.1073/pnas.91.16.7618;
RA Stasiak A., Tsaneva I.R., West S.C., Benson C.J., Yu X., Egelman E.H.;
RT "The Escherichia coli RuvB branch migration protein forms double hexameric
RT rings around DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7618-7622(1994).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=7885479; DOI=10.1038/374375a0;
RA Parsons C.A., Stasiak A., Bennett R.J., West S.C.;
RT "Structure of a multisubunit complex that promotes DNA branch migration.";
RL Nature 374:375-378(1995).
RN [18]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9078376; DOI=10.1046/j.1365-2443.1996.d01-253.x;
RA Hiom K., Tsaneva I.R., West S.C.;
RT "The directionality of RuvAB-mediated branch migration: in vitro studies
RT with three-armed junctions.";
RL Genes Cells 1:443-451(1996).
RN [19]
RP FUNCTION, IN VITRO RECONSTITUTION, AND SUBUNIT.
RX PubMed=9160752; DOI=10.1016/s0092-8674(00)80242-1;
RA Eggleston A.K., Mitchell A.H., West S.C.;
RT "In vitro reconstitution of the late steps of genetic recombination in E.
RT coli.";
RL Cell 89:607-617(1997).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=9047358; DOI=10.1006/jmbi.1996.0799;
RA Yu X., West S.C., Egelman E.H.;
RT "Structure and subunit composition of the RuvAB-Holliday junction
RT complex.";
RL J. Mol. Biol. 266:217-222(1997).
RN [21]
RP HOLLIDAY JUNCTION-RUVABC COMPLEX FORMATION.
RX PubMed=9637927; DOI=10.1016/s0960-9822(98)70282-9;
RA Davies A.A., West S.C.;
RT "Formation of RuvABC-Holliday junction complexes in vitro.";
RL Curr. Biol. 8:725-727(1998).
RN [22]
RP ROLE IN REPLICATION FORK REVERSAL, AND DISRUPTION PHENOTYPE.
RX PubMed=9814711; DOI=10.1016/s0092-8674(00)81772-9;
RA Seigneur M., Bidnenko V., Ehrlich S.D., Michel B.;
RT "RuvAB acts at arrested replication forks.";
RL Cell 95:419-430(1998).
RN [23]
RP FUNCTION, IN VITRO RECONSTITUTION, AND SUBUNIT.
RX PubMed=10421637; DOI=10.1101/gad.13.14.1861;
RA van Gool A.J., Hajibagheri N.M., Stasiak A., West S.C.;
RT "Assembly of the Escherichia coli RuvABC resolvasome directs the
RT orientation of holliday junction resolution.";
RL Genes Dev. 13:1861-1870(1999).
RN [24]
RP FUNCTION ON CROSS-LINKED DNA.
RX PubMed=10662672; DOI=10.1016/s0960-9822(00)00296-7;
RA George H., Kuraoka I., Nauman D.A., Kobertz W.R., Wood R.D., West S.C.;
RT "RuvAB-mediated branch migration does not involve extensive DNA opening
RT within the RuvB hexamer.";
RL Curr. Biol. 10:103-106(2000).
RN [25]
RP ROLE IN REPLICATION FORK REVERSAL.
RX PubMed=16424908; DOI=10.1038/sj.emboj.7600941;
RA Baharoglu Z., Petranovic M., Flores M.J., Michel B.;
RT "RuvAB is essential for replication forks reversal in certain replication
RT mutants.";
RL EMBO J. 25:596-604(2006).
RN [26]
RP ROLE IN REPLICATION FORK REVERSAL, ROLE IN MITOMYCIN C RESISTANCE, AND
RP MUTAGENESIS OF ALA-22; TYR-184; PRO-220 AND ALA-250.
RX PubMed=18942176; DOI=10.1111/j.1365-2958.2008.06431.x;
RA Le Masson M., Baharoglu Z., Michel B.;
RT "ruvA and ruvB mutants specifically impaired for replication fork
RT reversal.";
RL Mol. Microbiol. 70:537-548(2008).
RN [27]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [28]
RP INTERACTION WITH CAS1 (YGBT), AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=21219465; DOI=10.1111/j.1365-2958.2010.07465.x;
RA Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B.,
RA Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S.,
RA Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J.,
RA Edwards A.M., Yakunin A.F.;
RT "A dual function of the CRISPR-Cas system in bacterial antivirus immunity
RT and DNA repair.";
RL Mol. Microbiol. 79:484-502(2011).
CC -!- FUNCTION: The RuvABC complex is involved in recombinational repair of
CC UV or chemically damaged DNA (PubMed:6374379). The RuvAB complex also
CC plays an important role in the rescue of blocked DNA replication forks
CC via replication fork reversal (RFR); RFR and homologous recombination
CC required for UV light survival can be separated (PubMed:9814711,
CC PubMed:16424908, PubMed:18942176). This subunit has a weak ATPase
CC activity that is inhibited by its ADP product; binds ADP better than
CC ATP (PubMed:2529252). Promotes Holliday junction (HJ) branch migration
CC in conjunction with RuvA. Binds to HJ cruciform DNA; in the presence of
CC RuvA, ATP and Mg(2+) the junction is dissociated. Hydrolyzable (d)NTPs
CC can replace ATP but other analogs cannot (PubMed:1617728,
CC PubMed:6374379, PubMed:1608954, PubMed:8393934). The RuvB hexamer acts
CC as a pump, pulling DNA into and through the RuvAB complex
CC (PubMed:9078376). Can bypass UV-induced lesions (PubMed:1617728) and
CC physically cross-linked DNA strands (PubMed:10662672), suggesting RuvB
CC does not unwind large sections of DNA. RuvA gives specificity by
CC binding to cruciform junctions, while the RuvB ATPase provides the
CC motor force for branch migration; excess RuvB can promote branch
CC migration in the absence of RuvA (PubMed:1617728, PubMed:10662672). In
CC vitro the RuvA-RuvB complex has 5'-3' helicase activity that is ATP-
CC dependent and works best on short dsDNA hybrids; 52 and 66-nucleotide
CC (nt) pairs are easily displaced, hybrids greater than 140-nts are not
CC (PubMed:8433990). RuvA stimulates the weak ATPase activity of RuvB in
CC the presence of DNA; HJ DNA stimulates ATPase about 10-fold
CC (PubMed:1833759, PubMed:1435721, PubMed:8393934). {ECO:0000255|HAMAP-
CC Rule:MF_00016, ECO:0000269|PubMed:10662672, ECO:0000269|PubMed:1435721,
CC ECO:0000269|PubMed:1608954, ECO:0000269|PubMed:1617728,
CC ECO:0000269|PubMed:16424908, ECO:0000269|PubMed:1833759,
CC ECO:0000269|PubMed:18942176, ECO:0000269|PubMed:2529252,
CC ECO:0000269|PubMed:6374379, ECO:0000269|PubMed:8393934,
CC ECO:0000269|PubMed:8433990, ECO:0000269|PubMed:9078376,
CC ECO:0000269|PubMed:9814711}.
CC -!- FUNCTION: An in vitro resolvase system that forms and processes HJ has
CC been reconstituted with DNA substrates, RuvA, RuvB and RuvC. RuvA-RuvB
CC increases the rate of strand exchange (branch migration), dissociates
CC the RecA filament and allows RuvC to cleave in both orientations at the
CC cruciform junction (PubMed:9160752, PubMed:10421637). HJ-RuvA-RuvB-RuvC
CC complexes resolve Holliday junctions and also undergo branch migration,
CC providing evidence for a coupled branch migration/HJ resolution
CC reaction (PubMed:10421637). {ECO:0000269|PubMed:10421637,
CC ECO:0000269|PubMed:9160752}.
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 ECO:0000269|PubMed:8433990};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1617728};
CC Note=Branch migration by the RuvA-RuvB complex requires Mg(2+).
CC {ECO:0000269|PubMed:1617728};
CC -!- ACTIVITY REGULATION: The ATPase activity is inhibited by the ADP
CC product. {ECO:0000269|PubMed:2529252}.
CC -!- SUBUNIT: Monomer in solution (PubMed:2529252). Homodimer in solution
CC (PubMed:1435721). Homohexamer (PubMed:8052630, PubMed:7885479,
CC PubMed:9078376). Forms a stable RuvA-RuvB-Holliday junction (HJ)
CC complex in the presence of non-hydrolyzable (d)NTPs; in the presence of
CC hydrolyzable (d)NTPs branch migration occurs (PubMed:8393934,
CC PubMed:7885479). Two oppositely facing RuvB hexamers sandwich possibly
CC 2 RuvA tetramers at cruciform DNA structures (PubMed:7885479,
CC PubMed:9047358). Homododecamer composed of two hexameric rings; when
CC bound to DNA in the presence of ATP-gamma-S and Mg(2+)
CC (PubMed:8052630). Forms a complex with RuvA without DNA. Forms a
CC complex with RuvC without DNA (PubMed:9160752). In the presence of HJ
CC DNA a (probably) DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms with 2
CC rings of RuvB that resolves upon addition of ATP. Upon resolution the
CC protein complex dissociates from DNA (PubMed:9637927, PubMed:10421637).
CC Interacts with Cas1 (ygbT) (PubMed:21219465). {ECO:0000255|HAMAP-
CC Rule:MF_00016, ECO:0000269|PubMed:10421637, ECO:0000269|PubMed:1435721,
CC ECO:0000269|PubMed:21219465, ECO:0000269|PubMed:2529252,
CC ECO:0000269|PubMed:7885479, ECO:0000269|PubMed:8052630,
CC ECO:0000269|PubMed:8393934, ECO:0000269|PubMed:9047358,
CC ECO:0000269|PubMed:9160752, ECO:0000269|PubMed:9637927}.
CC -!- INTERACTION:
CC P0A812; P0A809: ruvA; NbExp=5; IntAct=EBI-557878, EBI-555119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00016,
CC ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete
CC nucleoid foci (probable DNA damage sites) upon treatment with mitomycin
CC C (MMC) for 2 hours.
CC -!- INDUCTION: Part of the ruvA-ruvB operon. Expression of the ruv region
CC is induced by damage to DNA and is regulated by LexA as part of the SOS
CC response. RuvA and RuvB are also involved in mutagenesis induced by UV
CC and X irradiation and by some chemicals (PubMed:3279394,
CC PubMed:2842314). Induced by hydroxyurea (PubMed:20005847).
CC {ECO:0000269|PubMed:20005847, ECO:0000269|PubMed:2842314,
CC ECO:0000269|PubMed:3279394}.
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:0000255|HAMAP-Rule:MF_00016}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to radiation, filamentous growth after
CC transient inhibition of DNA synthesis, little effect on conjugal
CC recombination in wild-type strains (PubMed:6374379). Increased
CC sensitivity to mitomycin and UV light (PubMed:2693946, PubMed:2164626).
CC Suppresses lethality in recB-recC and dnaB temperature-sensitive
CC mutants (PubMed:9814711). {ECO:0000269|PubMed:2164626,
CC ECO:0000269|PubMed:2693946, ECO:0000269|PubMed:6374379,
CC ECO:0000269|PubMed:9814711}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
CC -!- CAUTION: While this subunit has weak helicase activity in vitro
CC (PubMed:8433990), it does not act as one in vivo but rather as an ATP-
CC dependent pump that drives DNA passage through the RuvA-RuvB complex to
CC promote Holliday junction branch migration.
CC {ECO:0000269|PubMed:10662672, ECO:0000269|PubMed:1617728,
CC ECO:0000269|PubMed:8433990}.
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DR EMBL; X07091; CAA30120.1; -; Genomic_DNA.
DR EMBL; M21298; AAA24613.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74930.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15671.1; -; Genomic_DNA.
DR PIR; B28533; BVECVB.
DR RefSeq; NP_416374.1; NC_000913.3.
DR RefSeq; WP_000568519.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P0A812; -.
DR SMR; P0A812; -.
DR BioGRID; 4260882; 85.
DR ComplexPortal; CPX-5124; RuvAB Holliday junction DNA helicase complex.
DR DIP; DIP-47870N; -.
DR IntAct; P0A812; 18.
DR STRING; 511145.b1860; -.
DR jPOST; P0A812; -.
DR PaxDb; 511145-b1860; -.
DR EnsemblBacteria; AAC74930; AAC74930; b1860.
DR GeneID; 75202735; -.
DR GeneID; 946371; -.
DR KEGG; ecj:JW1849; -.
DR KEGG; eco:b1860; -.
DR PATRIC; fig|1411691.4.peg.388; -.
DR EchoBASE; EB0917; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_6; -.
DR InParanoid; P0A812; -.
DR OMA; IHRMSRP; -.
DR OrthoDB; 9804478at2; -.
DR PhylomeDB; P0A812; -.
DR BioCyc; EcoCyc:EG10924-MONOMER; -.
DR BioCyc; MetaCyc:EG10924-MONOMER; -.
DR PRO; PR:P0A812; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009379; C:Holliday junction helicase complex; IPI:ComplexPortal.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IDA:CACAO.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009378; F:four-way junction helicase activity; IDA:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; IDA:ComplexPortal.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome; SOS response.
FT CHAIN 1..336
FT /note="Holliday junction branch migration complex subunit
FT RuvB"
FT /id="PRO_0000165528"
FT REGION 4..184
FT /note="Large ATPase domain (RuvB-L)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT REGION 185..255
FT /note="Small ATPAse domain (RuvB-S)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT REGION 258..336
FT /note="Head domain (RuvB-H)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 131..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 294
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 313
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT BINDING 318
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT MUTAGEN 22
FT /note="A->V: Defective replication fork reversal (RFR), UV
FT light resistant, resistant to mitomycin C (MMC)."
FT /evidence="ECO:0000269|PubMed:18942176"
FT MUTAGEN 184
FT /note="Y->H: Defective RFR, UV light resistant, resistant
FT to MMC."
FT /evidence="ECO:0000269|PubMed:18942176"
FT MUTAGEN 220
FT /note="P->S: Defective RFR, UV light resistant, variably
FT resistant to MMC."
FT /evidence="ECO:0000269|PubMed:18942176"
FT MUTAGEN 250
FT /note="A->T: Defective RFR, UV light resistant, sensitive
FT to MMC."
FT /evidence="ECO:0000269|PubMed:18942176"
SQ SEQUENCE 336 AA; 37174 MW; 79BAB4A9A5687F7C CRC64;
MIEADRLISA GTTLPEDVAD RAIRPKLLEE YVGQPQVRSQ MEIFIKAAKL RGDALDHLLI
FGPPGLGKTT LANIVANEMG VNLRTTSGPV LEKAGDLAAM LTNLEPHDVL FIDEIHRLSP
VVEEVLYPAM EDYQLDIMIG EGPAARSIKI DLPPFTLIGA TTRAGSLTSP LRDRFGIVQR
LEFYQVPDLQ YIVSRSARFM GLEMSDDGAL EVARRARGTP RIANRLLRRV RDFAEVKHDG
TISADIAAQA LDMLNVDAEG FDYMDRKLLL AVIDKFFGGP VGLDNLAAAI GEERETIEDV
LEPYLIQQGF LQRTPRGRMA TTRAWNHFGI TPPEMP
//
