RUVA_ECOLI
ID RUVA_ECOLI Reviewed; 203 AA.
AC P0A809; P08576;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031};
GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031};
GN OrderedLocusNames=b1861, JW1850;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=1885548; DOI=10.1128/jb.173.18.5747-5753.1991;
RA Takahagi M., Iwasaki H., Nakata A., Shinagawa H.;
RT "Molecular analysis of the Escherichia coli ruvC gene, which encodes a
RT Holliday junction-specific endonuclease.";
RL J. Bacteriol. 173:5747-5753(1991).
RN [7]
RP FUNCTION, 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 [8]
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 [9]
RP 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=8832889; DOI=10.1126/science.274.5286.415;
RA Rafferty J.B., Sedelnikova S.E., Hargreaves D., Artymiuk P.J., Baker P.J.,
RA Sharples G.J., Mahdi A.A., Lloyd R.G., Rice D.W.;
RT "Crystal structure of DNA recombination protein RuvA and a model for its
RT binding to the Holliday junction.";
RL Science 274:415-421(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
RX PubMed=9628481; DOI=10.1038/nsb0698-441;
RA Hargreaves D., Rice D.W., Sedelnikova S.E., Artymiuk P.J., Lloyd R.G.,
RA Rafferty J.B.;
RT "Crystal structure of E.coli RuvA with bound DNA Holliday junction at 6-A
RT resolution.";
RL Nat. Struct. Biol. 5:441-446(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=9493263; DOI=10.1016/s0969-2126(98)00003-3;
RA Nishino T., Ariyoshi M., Iwasaki H., Shinagawa H., Morikawa K.;
RT "Functional analyses of the domain structure in the Holliday junction
RT binding protein RuvA.";
RL Structure 6:11-21(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-149.
RX PubMed=10772859; DOI=10.1006/jmbi.2000.3675;
RA Nishino T., Iwasaki H., Kataoka M., Ariyoshi M., Fujita T., Shinagawa H.,
RA Morikawa K.;
RT "Modulation of RuvB function by the mobile domain III of the Holliday
RT junction recognition protein RuvA.";
RL J. Mol. Biol. 298:407-416(2000).
RN [14]
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. RuvA stimulates,
CC in the presence of DNA, the weak ATPase activity of RuvB. Binds both
CC single- and double-stranded DNA (dsDNA). Binds preferentially to
CC supercoiled rather than to relaxed dsDNA. {ECO:0000255|HAMAP-
CC Rule:MF_00031, 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_00031,
CC ECO:0000269|PubMed:8433990};
CC -!- SUBUNIT: Homotetramer; forms a complex with RuvB.
CC {ECO:0000269|PubMed:8832889, ECO:0000269|PubMed:9493263}.
CC -!- INTERACTION:
CC P0A809; P0A809: ruvA; NbExp=5; IntAct=EBI-555119, EBI-555119;
CC P0A809; P0A812: ruvB; NbExp=5; IntAct=EBI-555119, EBI-557878;
CC P0A809; P0A814: ruvC; NbExp=4; IntAct=EBI-555119, EBI-1123014;
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 RuvA family. {ECO:0000255|HAMAP-
CC Rule:MF_00031}.
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DR EMBL; X07091; CAA30119.1; -; Genomic_DNA.
DR EMBL; M21298; AAA24612.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74931.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15672.1; -; Genomic_DNA.
DR EMBL; D10165; BAA01034.1; -; Genomic_DNA.
DR PIR; E64948; BVECRV.
DR RefSeq; NP_416375.1; NC_000913.3.
DR RefSeq; WP_000580323.1; NZ_STEB01000009.1.
DR PDB; 1BDX; X-ray; 6.00 A; A/B/C/D=1-203.
DR PDB; 1C7Y; X-ray; 3.10 A; A=1-203.
DR PDB; 1CUK; X-ray; 1.90 A; A=1-203.
DR PDB; 1D8L; X-ray; 2.50 A; A/B=1-149.
DR PDB; 1HJP; X-ray; 2.50 A; A=1-203.
DR PDBsum; 1BDX; -.
DR PDBsum; 1C7Y; -.
DR PDBsum; 1CUK; -.
DR PDBsum; 1D8L; -.
DR PDBsum; 1HJP; -.
DR AlphaFoldDB; P0A809; -.
DR SMR; P0A809; -.
DR BioGRID; 4259338; 146.
DR BioGRID; 850726; 1.
DR ComplexPortal; CPX-5124; RuvAB Holliday junction DNA helicase complex.
DR DIP; DIP-48064N; -.
DR IntAct; P0A809; 9.
DR STRING; 511145.b1861; -.
DR jPOST; P0A809; -.
DR PaxDb; P0A809; -.
DR PRIDE; P0A809; -.
DR EnsemblBacteria; AAC74931; AAC74931; b1861.
DR EnsemblBacteria; BAA15672; BAA15672; BAA15672.
DR GeneID; 66674249; -.
DR GeneID; 946369; -.
DR KEGG; ecj:JW1850; -.
DR KEGG; eco:b1861; -.
DR PATRIC; fig|1411691.4.peg.387; -.
DR EchoBASE; EB0916; -.
DR eggNOG; COG0632; Bacteria.
DR HOGENOM; CLU_087936_0_0_6; -.
DR InParanoid; P0A809; -.
DR OMA; VGMAVQC; -.
DR PhylomeDB; P0A809; -.
DR BioCyc; EcoCyc:EG10923-MON; -.
DR BioCyc; MetaCyc:EG10923-MON; -.
DR EvolutionaryTrace; P0A809; -.
DR PRO; PR:P0A809; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009379; C:Holliday junction helicase complex; IDA:EcoCyc.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:EcoCyc.
DR GO; GO:0009378; F:four-way junction helicase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; IDA:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR CDD; cd14332; UBA_RuvA_C; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00031; DNA_helic_RuvA; 1.
DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000085; RuvA.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR011114; RuvA_C.
DR InterPro; IPR036267; RuvA_C_sf.
DR Pfam; PF07499; RuvA_C; 1.
DR Pfam; PF01330; RuvA_N; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46929; SSF46929; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00084; ruvA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; SOS response.
FT CHAIN 1..203
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_0000094629"
FT CONFLICT 166
FT /note="A -> R (in Ref. 1; CAA30119)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:1CUK"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1CUK"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1CUK"
FT STRAND 43..54
FT /evidence="ECO:0007829|PDB:1CUK"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:1CUK"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1CUK"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:1C7Y"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1CUK"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1CUK"
SQ SEQUENCE 203 AA; 22086 MW; 805DDB79DC5A8385 CRC64;
MIGRLRGIII EKQPPLVLIE VGGVGYEVHM PMTCFYELPE AGQEAIVFTH FVVREDAQLL
YGFNNKQERT LFKELIKTNG VGPKLALAIL SGMSAQQFVN AVEREEVGAL VKLPGIGKKT
AERLIVEMKD RFKGLHGDLF TPAADLVLTS PASPATDDAE QEAVAALVAL GYKPQEASRM
VSKIARPDAS SETLIREALR AAL
