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Protein

Protein RecA

Gene

recA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for homologous recombination and the bypass of mutagenic DNA lesions by the SOS response. Catalyzes ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. Catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in response to DNA damaging agents that is mediated by RecA and LexA (PubMed:22412352).4 Publications

Enzyme regulationi

The rate of DNA-strand exchange is stimulated by RadA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 748ATPUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell motility Source: EcoliWiki
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • DNA recombinase assembly Source: GO_Central
  • DNA recombination Source: CACAO
  • mitotic recombination Source: GO_Central
  • response to ionizing radiation Source: EcoCyc
  • SOS response Source: CACAO
  • strand invasion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, SOS response, Stress response

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10823-MONOMER.
ECOL316407:JW2669-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RecAUniRule annotation
Alternative name(s):
Recombinase AUniRule annotation
Gene namesi
Name:recAUniRule annotation
Synonyms:lexB, recH, rnmB, tif, umuB, zab
Ordered Locus Names:b2699, JW2669
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10823. recA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Triple mazE-mazF-recA mutant cells no longer undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization (PubMed:22412352).

Chemistry

ChEMBLiCHEMBL3434.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 353352Protein RecAPRO_0000122703Add
BLAST

Proteomic databases

EPDiP0A7G6.
PaxDbiP0A7G6.
PRIDEiP0A7G6.

2D gel databases

SWISS-2DPAGEP0A7G6.

Expressioni

Inductioni

In response to low temperature. Sensitive to temperature through changes in the linking number of the DNA. 5.1-fold induced by hydroxyurea treatment (at protein level) (PubMed:20005847). mRNA levels are repressed in a mazE-mazF-mediated manner (PubMed:22412352).2 Publications

Interactioni

Subunit structurei

Polymerizes non-specifically on ssDNA to form filaments; filament formation requires ATP or ATP-gamma-S. Interacts with and activates LexA leading to autocatalytic cleavage of LexA, which derepresses the SOS regulon and activates DNA repair. Interacts with the C-terminus of RecB, facilitating loading of RecA onto ssDNA at chi sites. Interaction is decreased by ATP.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mutLP233673EBI-370331,EBI-554913

Protein-protein interaction databases

BioGridi4259218. 403 interactions.
DIPiDIP-31832N.
IntActiP0A7G6. 28 interactions.
MINTiMINT-1300726.
STRINGi511145.b2699.

Chemistry

BindingDBiP0A7G6.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2215Combined sources
Helixi24 – 263Combined sources
Beta strandi27 – 293Combined sources
Helixi30 – 323Combined sources
Helixi34 – 363Combined sources
Helixi46 – 516Combined sources
Beta strandi53 – 586Combined sources
Beta strandi61 – 666Combined sources
Helixi73 – 8614Combined sources
Beta strandi91 – 977Combined sources
Helixi102 – 1076Combined sources
Helixi112 – 1143Combined sources
Beta strandi116 – 1183Combined sources
Helixi123 – 13614Combined sources
Beta strandi140 – 1456Combined sources
Helixi147 – 1493Combined sources
Helixi153 – 1564Combined sources
Helixi167 – 18620Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi208 – 2125Combined sources
Helixi214 – 2196Combined sources
Beta strandi221 – 25333Combined sources
Beta strandi258 – 2647Combined sources
Turni265 – 2673Combined sources
Helixi271 – 28111Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi297 – 3026Combined sources
Helixi303 – 31210Combined sources
Helixi314 – 32815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA3NMR-A269-331[»]
1N03electron microscopy20.00A/B/C/D/E/F/G2-353[»]
1REAX-ray2.70A2-353[»]
1U94X-ray1.90A2-353[»]
1U98X-ray2.00A2-353[»]
1U99X-ray2.60A2-353[»]
1XMSX-ray2.10A2-353[»]
1XMVX-ray1.90A2-353[»]
2REBX-ray2.30A2-353[»]
2RECelectron microscopy-A/B/C/D/E/F1-353[»]
3CMTX-ray3.15A/D2-335[»]
3CMUX-ray4.20A2-335[»]
3CMVX-ray4.30A/B/C/D/E/F/G/H2-335[»]
3CMWX-ray2.80A/C2-335[»]
3CMXX-ray3.40A/D2-335[»]
4TWZX-ray2.80A2-353[»]
ProteinModelPortaliP0A7G6.
SMRiP0A7G6. Positions 7-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7G6.

Family & Domainsi

Sequence similaritiesi

Belongs to the RecA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C68. Bacteria.
COG0468. LUCA.
HOGENOMiHOG000264120.
InParanoidiP0A7G6.
KOiK03553.
OMAiPPFKEAH.
PhylomeDBiP0A7G6.

Family and domain databases

CDDicd00983. recA. 1 hit.
Gene3Di3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR22942:SF1. PTHR22942:SF1. 1 hit.
PfamiPF00154. RecA. 1 hit.
[Graphical view]
PRINTSiPR00142. RECA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
TIGRFAMsiTIGR02012. tigrfam_recA. 1 hit.
PROSITEiPS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7G6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI
60 70 80 90 100
ALGAGGLPMG RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL
110 120 130 140 150
DPIYARKLGV DIDNLLCSQP DTGEQALEIC DALARSGAVD VIVVDSVAAL
160 170 180 190 200
TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA GNLKQSNTLL IFINQIRMKI
210 220 230 240 250
GVMFGNPETT TGGNALKFYA SVRLDIRRIG AVKEGENVVG SETRVKVVKN
260 270 280 290 300
KIAAPFKQAE FQILYGEGIN FYGELVDLGV KEKLIEKAGA WYSYKGEKIG
310 320 330 340 350
QGKANATAWL KDNPETAKEI EKKVRELLLS NPNSTPDFSV DDSEGVAETN

EDF
Length:353
Mass (Da):37,973
Last modified:January 23, 2007 - v2
Checksum:i866EF8F83BE32A36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911Missing AA sequence (PubMed:7588783).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00328 Genomic DNA. Translation: CAA23618.1.
U00096 Genomic DNA. Translation: AAC75741.1.
AP009048 Genomic DNA. Translation: BAA16561.2.
PIRiG65049. RQECA.
RefSeqiNP_417179.1. NC_000913.3.
WP_000963143.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75741; AAC75741; b2699.
BAA16561; BAA16561; BAA16561.
GeneIDi947170.
KEGGiecj:JW2669.
eco:b2699.
PATRICi32120796. VBIEscCol129921_2790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00328 Genomic DNA. Translation: CAA23618.1.
U00096 Genomic DNA. Translation: AAC75741.1.
AP009048 Genomic DNA. Translation: BAA16561.2.
PIRiG65049. RQECA.
RefSeqiNP_417179.1. NC_000913.3.
WP_000963143.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA3NMR-A269-331[»]
1N03electron microscopy20.00A/B/C/D/E/F/G2-353[»]
1REAX-ray2.70A2-353[»]
1U94X-ray1.90A2-353[»]
1U98X-ray2.00A2-353[»]
1U99X-ray2.60A2-353[»]
1XMSX-ray2.10A2-353[»]
1XMVX-ray1.90A2-353[»]
2REBX-ray2.30A2-353[»]
2RECelectron microscopy-A/B/C/D/E/F1-353[»]
3CMTX-ray3.15A/D2-335[»]
3CMUX-ray4.20A2-335[»]
3CMVX-ray4.30A/B/C/D/E/F/G/H2-335[»]
3CMWX-ray2.80A/C2-335[»]
3CMXX-ray3.40A/D2-335[»]
4TWZX-ray2.80A2-353[»]
ProteinModelPortaliP0A7G6.
SMRiP0A7G6. Positions 7-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259218. 403 interactions.
DIPiDIP-31832N.
IntActiP0A7G6. 28 interactions.
MINTiMINT-1300726.
STRINGi511145.b2699.

Chemistry

BindingDBiP0A7G6.
ChEMBLiCHEMBL3434.

2D gel databases

SWISS-2DPAGEP0A7G6.

Proteomic databases

EPDiP0A7G6.
PaxDbiP0A7G6.
PRIDEiP0A7G6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75741; AAC75741; b2699.
BAA16561; BAA16561; BAA16561.
GeneIDi947170.
KEGGiecj:JW2669.
eco:b2699.
PATRICi32120796. VBIEscCol129921_2790.

Organism-specific databases

EchoBASEiEB0816.
EcoGeneiEG10823. recA.

Phylogenomic databases

eggNOGiENOG4105C68. Bacteria.
COG0468. LUCA.
HOGENOMiHOG000264120.
InParanoidiP0A7G6.
KOiK03553.
OMAiPPFKEAH.
PhylomeDBiP0A7G6.

Enzyme and pathway databases

BioCyciEcoCyc:EG10823-MONOMER.
ECOL316407:JW2669-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7G6.
PROiP0A7G6.

Family and domain databases

CDDicd00983. recA. 1 hit.
Gene3Di3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR013765. DNA_recomb/repair_RecA.
IPR020584. DNA_recomb/repair_RecA_CS.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR023400. RecA_C.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PANTHERiPTHR22942:SF1. PTHR22942:SF1. 1 hit.
PfamiPF00154. RecA. 1 hit.
[Graphical view]
PRINTSiPR00142. RECA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
TIGRFAMsiTIGR02012. tigrfam_recA. 1 hit.
PROSITEiPS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRECA_ECOLI
AccessioniPrimary (citable) accession number: P0A7G6
Secondary accession number(s): P03017, P26347, P78213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.