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Protein

Holliday junction ATP-dependent DNA helicase RuvA

Gene

ruvA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.UniRule annotation1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • four-way junction DNA binding Source: EcoCyc
  • four-way junction helicase activity Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

  • protein homotetramerization Source: EcoCyc
  • recombinational repair Source: EcoCyc
  • response to radiation Source: EcoCyc
  • SOS response Source: EcoCyc

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA recombination, DNA repair, SOS response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10923-MONOMER
MetaCyc:EG10923-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Holliday junction ATP-dependent DNA helicase RuvAUniRule annotation (EC:3.6.4.12UniRule annotation)
Gene namesi
Name:ruvAUniRule annotation
Ordered Locus Names:b1861, JW1850
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10923 ruvA

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000946291 – 203Holliday junction ATP-dependent DNA helicase RuvAAdd BLAST203

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 (PubMed:3279394). Induced by hydroxyurea (PubMed:20005847).2 Publications

Interactioni

Subunit structurei

Homotetramer; forms a complex with RuvB.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-555119,EBI-555119

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4259338, 146 interactors
DIPiDIP-48064N
IntActiP0A809, 8 interactors
STRINGi316385.ECDH10B_2002

Structurei

Secondary structure

1203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A809
SMRiP0A809
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A809

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105KA4 Bacteria
COG0632 LUCA
HOGENOMiHOG000057116
InParanoidiP0A809
KOiK03550
PhylomeDBiP0A809

Family and domain databases

CDDicd14332 UBA_RuvA_C, 1 hit
HAMAPiMF_00031 DNA_helic_RuvA, 1 hit
InterProiView protein in InterPro
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
IPR011114 RuvA_C
IPR036267 RuvA_C_sf
PANTHERiPTHR33796 PTHR33796, 1 hit
PfamiView protein in Pfam
PF07499 RuvA_C, 1 hit
PF01330 RuvA_N, 1 hit
SMARTiView protein in SMART
SM00278 HhH1, 2 hits
SUPFAMiSSF46929 SSF46929, 1 hit
SSF47781 SSF47781, 1 hit
SSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR00084 ruvA, 1 hit

Sequencei

Sequence statusi: Complete.

P0A809-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIGRLRGIII EKQPPLVLIE VGGVGYEVHM PMTCFYELPE AGQEAIVFTH
60 70 80 90 100
FVVREDAQLL YGFNNKQERT LFKELIKTNG VGPKLALAIL SGMSAQQFVN
110 120 130 140 150
AVEREEVGAL VKLPGIGKKT AERLIVEMKD RFKGLHGDLF TPAADLVLTS
160 170 180 190 200
PASPATDDAE QEAVAALVAL GYKPQEASRM VSKIARPDAS SETLIREALR

AAL
Length:203
Mass (Da):22,086
Last modified:June 7, 2005 - v1
Checksum:i805DDB79DC5A8385
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166A → R in CAA30119 (PubMed:3279394).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
PIRiE64948 BVECRV
RefSeqiNP_416375.1, NC_000913.3
WP_000580323.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74931; AAC74931; b1861
BAA15672; BAA15672; BAA15672
GeneIDi946369
KEGGiecj:JW1850
eco:b1861
PATRICifig|1411691.4.peg.387

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
PIRiE64948 BVECRV
RefSeqiNP_416375.1, NC_000913.3
WP_000580323.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259338, 146 interactors
DIPiDIP-48064N
IntActiP0A809, 8 interactors
STRINGi316385.ECDH10B_2002

Proteomic databases

PaxDbiP0A809
PRIDEiP0A809

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74931; AAC74931; b1861
BAA15672; BAA15672; BAA15672
GeneIDi946369
KEGGiecj:JW1850
eco:b1861
PATRICifig|1411691.4.peg.387

Organism-specific databases

EchoBASEiEB0916
EcoGeneiEG10923 ruvA

Phylogenomic databases

eggNOGiENOG4105KA4 Bacteria
COG0632 LUCA
HOGENOMiHOG000057116
InParanoidiP0A809
KOiK03550
PhylomeDBiP0A809

Enzyme and pathway databases

BioCyciEcoCyc:EG10923-MONOMER
MetaCyc:EG10923-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A809
PROiPR:P0A809

Family and domain databases

CDDicd14332 UBA_RuvA_C, 1 hit
HAMAPiMF_00031 DNA_helic_RuvA, 1 hit
InterProiView protein in InterPro
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
IPR011114 RuvA_C
IPR036267 RuvA_C_sf
PANTHERiPTHR33796 PTHR33796, 1 hit
PfamiView protein in Pfam
PF07499 RuvA_C, 1 hit
PF01330 RuvA_N, 1 hit
SMARTiView protein in SMART
SM00278 HhH1, 2 hits
SUPFAMiSSF46929 SSF46929, 1 hit
SSF47781 SSF47781, 1 hit
SSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR00084 ruvA, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRUVA_ECOLI
AccessioniPrimary (citable) accession number: P0A809
Secondary accession number(s): P08576
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 7, 2005
Last modified: November 7, 2018
This is version 112 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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