RUVB_ECOLI
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 03-AUG-2022, entry version 138.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016};
GN OrderedLocusNames=b1860, JW1849;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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]
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]
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]
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 FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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 [7]
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 [8]
RP INTERACTION WITH 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).
RN [9]
RP REVIEW.
RX PubMed=9442895; DOI=10.1146/annurev.genet.31.1.213;
RA West S.C.;
RT "Processing of recombination intermediates by the RuvABC proteins.";
RL Annu. Rev. Genet. 31:213-244(1997).
CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC cruciform structure in supercoiled DNA with palindromic sequence,
CC indicating that it may promote strand exchange reactions in homologous
CC recombination. RuvAB is a helicase that mediates the Holliday junction
CC migration by localized denaturation and reannealing.
CC {ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:8433990}.
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 -!- ACTIVITY REGULATION: RuvB possesses weak ATPase activity, which is
CC stimulated by the RuvA protein in the presence of DNA.
CC {ECO:0000269|PubMed:8433990}.
CC -!- SUBUNIT: Homododecamer composed of two hexameric rings; when bound to
CC DNA in the presence of ATP and magnesium. Forms a complex with RuvA.
CC Interacts with YgbT (Cas1). {ECO:0000269|PubMed:21219465}.
CC -!- INTERACTION:
CC P0A812; P0A809: ruvA; NbExp=5; IntAct=EBI-557878, EBI-555119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21219465}. Note=In
CC 15% of cell localizes to discrete nucleoid foci (probable DNA damage
CC sites) upon treatment with mitomycin C (MMC) for 2 hours.
CC -!- INDUCTION: Expression of the ruv region is induced by damage to DNA and
CC is regulated by LexA as part of the SOS response. RuvA and RuvB are
CC also involved in mutagenesis induced by UV and X irradiation and by
CC some chemicals (PubMed:3279394). Induced by hydroxyurea
CC (PubMed:20005847). {ECO:0000269|PubMed:20005847,
CC ECO:0000269|PubMed:3279394}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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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; P0A812; -.
DR PRIDE; P0A812; -.
DR EnsemblBacteria; AAC74930; AAC74930; b1860.
DR EnsemblBacteria; BAA15671; BAA15671; BAA15671.
DR GeneID; 66674250; -.
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 PhylomeDB; P0A812; -.
DR BioCyc; EcoCyc:EG10924-MON; -.
DR BioCyc; MetaCyc:EG10924-MON; -.
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:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IDA:CACAO.
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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00016; DNA_helic_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 PANTHER; PTHR42848; PTHR42848; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00635; ruvB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..336
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000165528"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
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
