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P0A809

- RUVA_ECOLI

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Protein
Holliday junction ATP-dependent DNA helicase RuvA
Gene
ruvA, b1861, JW1850

Gene:

ruvA, b1861, JW1850
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

UniProt

P0A809 - RUVA_ECOLI

Protein:

Holliday junction ATP-dependent DNA helicase RuvA
Protein Existence: Experimental evidence at protein level

Functioni

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. DNA bindingInferred from electronic annotationi Source: UniProtKB-KW
  3. four-way junction helicase activityInferred from direct assayi PubMed 1617728 Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. DNA bindingInferred from electronic annotationi Source: UniProtKB-KW
  3. four-way junction helicase activityInferred from direct assayi PubMed 1617728 Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, SOS response

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10923-MONOMER.
ECOL316407:JW1850-MONOMER.
MetaCyc:EG10923-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Holliday junction ATP-dependent DNA helicase RuvA (EC:3.6.4.12)
Gene namesi
Name:ruvA
Ordered Locus Names:b1861, JW1850
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10923. ruvA.

Subcellular locationi

Cytoplasm
Note: In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.1 Publication

GO - Cellular componenti

  1. Holliday junction helicase complexInferred from direct assayi PubMed 1617728 Source: EcoCyc
  2. Holliday junction resolvase complexInferred from direct assayi PubMed 9160752 Source: EcoCyc
  3. cytoplasmInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Chaini1 – 203203Holliday junction ATP-dependent DNA helicase RuvAUniRule annotation
PRO_0000094629

Proteomic databases

PaxDbiP0A809.
PRIDEiP0A809.

Expressioni

Inductioni

Expression of the ruv region is induced by damage to DNA and is regulated by LexA as part of the SOS response. RuvA and RuvB are also involved in mutagenesis induced by UV and X irradiation and by some chemicals.1 Publication

Gene expression databases

GenevestigatoriP0A809.

Interactioni

Subunit structurei

Homotetramer; forms a complex with RuvB.2 Publications

Protein-protein interaction databases

DIPiDIP-48064N.
IntActiP0A809. 7 interactions.
MINTiMINT-1321234.
STRINGi511145.b1861.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Beta strandi4 – 1310
Beta strandi16 – 216
Beta strandi24 – 296
Helixi32 – 354
Beta strandi43 – 5412
Beta strandi57 – 659
Helixi66 – 7712
Beta strandi78 – 803
Helixi83 – 9210
Helixi95 – 1039
Helixi107 – 1115
Helixi118 – 13114
Helixi132 – 1343
Turni138 – 1403
Helixi144 – 1496
Helixi158 – 17013
Helixi174 – 18310
Helixi191 – 20010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDXX-ray6.00A/B/C/D1-203[»]
1C7YX-ray3.10A1-203[»]
1CUKX-ray1.90A1-203[»]
1D8LX-ray2.50A/B1-149[»]
1HJPX-ray2.50A1-203[»]
ProteinModelPortaliP0A809.
SMRiP0A809. Positions 1-203.

Miscellaneous databases

EvolutionaryTraceiP0A809.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvA family.

Phylogenomic databases

eggNOGiCOG0632.
HOGENOMiHOG000057116.
KOiK03550.
OMAiVGYQVHC.
OrthoDBiEOG679THG.
PhylomeDBiP0A809.
ProtClustDBiPRK00116.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00031. DNA_helic_RuvA.
InterProiIPR011114. DNA_helicas_Holl-junc_RuvA_C.
IPR013849. DNA_helicase_Holl-junc_RuvA_I.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR000085. RuvA.
IPR010994. RuvA_2-like.
[Graphical view]
PfamiPF07499. RuvA_C. 1 hit.
PF01330. RuvA_N. 1 hit.
[Graphical view]
SMARTiSM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF46929. SSF46929. 1 hit.
SSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00084. ruvA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A809-1 [UniParc]FASTA

« Hide

MIGRLRGIII EKQPPLVLIE VGGVGYEVHM PMTCFYELPE AGQEAIVFTH    50
FVVREDAQLL YGFNNKQERT LFKELIKTNG VGPKLALAIL SGMSAQQFVN 100
AVEREEVGAL VKLPGIGKKT AERLIVEMKD RFKGLHGDLF TPAADLVLTS 150
PASPATDDAE QEAVAALVAL GYKPQEASRM VSKIARPDAS SETLIREALR 200
AAL 203
Length:203
Mass (Da):22,086
Last modified:June 7, 2005 - v1
Checksum:i805DDB79DC5A8385
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti1661A → R in CAA30119. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07091 Genomic DNA. Translation: CAA30119.1.
M21298 Genomic DNA. Translation: AAA24612.1.
U00096 Genomic DNA. Translation: AAC74931.1.
AP009048 Genomic DNA. Translation: BAA15672.1.
D10165 Genomic DNA. Translation: BAA01034.1.
PIRiBVECRV. E64948.
RefSeqiNP_416375.1. NC_000913.3.
YP_490123.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74931; AAC74931; b1861.
BAA15672; BAA15672; BAA15672.
GeneIDi12930344.
946369.
KEGGiecj:Y75_p1837.
eco:b1861.
PATRICi32119045. VBIEscCol129921_1940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07091 Genomic DNA. Translation: CAA30119.1 .
M21298 Genomic DNA. Translation: AAA24612.1 .
U00096 Genomic DNA. Translation: AAC74931.1 .
AP009048 Genomic DNA. Translation: BAA15672.1 .
D10165 Genomic DNA. Translation: BAA01034.1 .
PIRi BVECRV. E64948.
RefSeqi NP_416375.1. NC_000913.3.
YP_490123.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BDX X-ray 6.00 A/B/C/D 1-203 [» ]
1C7Y X-ray 3.10 A 1-203 [» ]
1CUK X-ray 1.90 A 1-203 [» ]
1D8L X-ray 2.50 A/B 1-149 [» ]
1HJP X-ray 2.50 A 1-203 [» ]
ProteinModelPortali P0A809.
SMRi P0A809. Positions 1-203.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-48064N.
IntActi P0A809. 7 interactions.
MINTi MINT-1321234.
STRINGi 511145.b1861.

Proteomic databases

PaxDbi P0A809.
PRIDEi P0A809.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74931 ; AAC74931 ; b1861 .
BAA15672 ; BAA15672 ; BAA15672 .
GeneIDi 12930344.
946369.
KEGGi ecj:Y75_p1837.
eco:b1861.
PATRICi 32119045. VBIEscCol129921_1940.

Organism-specific databases

EchoBASEi EB0916.
EcoGenei EG10923. ruvA.

Phylogenomic databases

eggNOGi COG0632.
HOGENOMi HOG000057116.
KOi K03550.
OMAi VGYQVHC.
OrthoDBi EOG679THG.
PhylomeDBi P0A809.
ProtClustDBi PRK00116.

Enzyme and pathway databases

BioCyci EcoCyc:EG10923-MONOMER.
ECOL316407:JW1850-MONOMER.
MetaCyc:EG10923-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A809.
PROi P0A809.

Gene expression databases

Genevestigatori P0A809.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
HAMAPi MF_00031. DNA_helic_RuvA.
InterProi IPR011114. DNA_helicas_Holl-junc_RuvA_C.
IPR013849. DNA_helicase_Holl-junc_RuvA_I.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR000085. RuvA.
IPR010994. RuvA_2-like.
[Graphical view ]
Pfami PF07499. RuvA_C. 1 hit.
PF01330. RuvA_N. 1 hit.
[Graphical view ]
SMARTi SM00278. HhH1. 2 hits.
[Graphical view ]
SUPFAMi SSF46929. SSF46929. 1 hit.
SSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00084. ruvA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publicationsDownload
  1. "Nucleotide sequencing of the ruv region of Escherichia coli K-12 reveals a LexA regulated operon encoding two genes."
    Benson F.E., Illing G.T., Sharples G.J., Lloyd R.G.
    Nucleic Acids Res. 16:1541-1549(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12.
  2. "Structure and regulation of the Escherichia coli ruv operon involved in DNA repair and recombination."
    Shinagawa H., Makino K., Amemura M., Kimura S., Iwasaki H., Nakata A.
    J. Bacteriol. 170:4322-4329(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
    Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.
    , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
    DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease."
    Takahagi M., Iwasaki H., Nakata A., Shinagawa H.
    J. Bacteriol. 173:5747-5753(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
  7. "RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro."
    Tsaneva I.R., Mueller B., West S.C.
    Proc. Natl. Acad. Sci. U.S.A. 90:1315-1319(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "A dual function of the CRISPR-Cas system in bacterial antivirus immunity and DNA repair."
    Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B., Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S., Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J., Edwards A.M., Yakunin A.F.
    Mol. Microbiol. 79:484-502(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12.
  9. "Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction."
    Rafferty J.B., Sedelnikova S.E., Hargreaves D., Artymiuk P.J., Baker P.J., Sharples G.J., Mahdi A.A., Lloyd R.G., Rice D.W.
    Science 274:415-421(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
  10. "Crystal structure of E.coli RuvA with bound DNA Holliday junction at 6-A resolution."
    Hargreaves D., Rice D.W., Sedelnikova S.E., Artymiuk P.J., Lloyd R.G., Rafferty J.B.
    Nat. Struct. Biol. 5:441-446(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
  11. "Functional analyses of the domain structure in the Holliday junction binding protein RuvA."
    Nishino T., Ariyoshi M., Iwasaki H., Shinagawa H., Morikawa K.
    Structure 6:11-21(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
  12. "Modulation of RuvB function by the mobile domain III of the Holliday junction recognition protein RuvA."
    Nishino T., Iwasaki H., Kataoka M., Ariyoshi M., Fujita T., Shinagawa H., Morikawa K.
    J. Mol. Biol. 298:407-416(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-149.
  13. "Processing of recombination intermediates by the RuvABC proteins."
    West S.C.
    Annu. Rev. Genet. 31:213-244(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry nameiRUVA_ECOLI
AccessioniPrimary (citable) accession number: P0A809
Secondary accession number(s): P08576
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

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