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P0A7G6 (RECA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein RecA
Alternative name(s):
Recombinase A
Gene names
Name:recA
Synonyms:lexB, recH, rnmB, tif, umuB, zab
Ordered Locus Names:b2699, JW2669
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Subunit structure

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. Ref.12 Ref.13

Subcellular location

Cytoplasm HAMAP-Rule MF_00268.

Induction

In response to low temperature. Sensitive to temperature through changes in the linking number of the DNA. HAMAP-Rule MF_00268

Sequence similarities

Belongs to the RecA family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mutLP233673EBI-370331,EBI-554913

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2
Chain2 – 353352Protein RecA HAMAP-Rule MF_00268
PRO_0000122703

Regions

Nucleotide binding67 – 748ATP HAMAP-Rule MF_00268

Experimental info

Sequence conflict1911Missing AA sequence Ref.8

Secondary structure

........................................................... 353
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7G6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 866EF8F83BE32A36

FASTA35337,973
        10         20         30         40         50         60 
MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI ALGAGGLPMG 

        70         80         90        100        110        120 
RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL DPIYARKLGV DIDNLLCSQP 

       130        140        150        160        170        180 
DTGEQALEIC DALARSGAVD VIVVDSVAAL TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA 

       190        200        210        220        230        240 
GNLKQSNTLL IFINQIRMKI GVMFGNPETT TGGNALKFYA SVRLDIRRIG AVKEGENVVG 

       250        260        270        280        290        300 
SETRVKVVKN KIAAPFKQAE FQILYGEGIN FYGELVDLGV KEKLIEKAGA WYSYKGEKIG 

       310        320        330        340        350 
QGKANATAWL KDNPETAKEI EKKVRELLLS NPNSTPDFSV DDSEGVAETN EDF 

« Hide

References

« Hide 'large scale' references
[1]"Organization of the recA gene of Escherichia coli."
Horii T., Ogawa T., Ogawa H.
Proc. Natl. Acad. Sci. U.S.A. 77:313-317(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6.
[2]"Sequences of the recA gene and protein."
Sancar A., Stachelek C., Konigsberg W., Rupp W.D.
Proc. Natl. Acad. Sci. U.S.A. 77:2611-2615(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-3.
[3]"DNA sequence analysis of the recA genes from Proteus vulgaris, Erwinia carotovora, Shigella flexneri and Escherichia coli B/r."
Zhao X.J., McEntee K.
Mol. Gen. Genet. 222:369-376(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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.
[6]"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], SEQUENCE REVISION TO 112.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"The DNA-binding site of the RecA protein. Photochemical cross-linking of Tyr103 to single-stranded DNA."
Morimatsu K., Horii T.
Eur. J. Biochem. 228:772-778(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 90-107 AND 179-184, DNA-BINDING.
[8]"The identification of the single-stranded DNA-binding domain of the Escherichia coli RecA protein."
Gardner R.V., Voloshin O.N., Camerini-Otero R.D.
Eur. J. Biochem. 233:419-425(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 187-194, DNA-BINDING.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Role of the Escherichia coli recombination hotspot, chi, in RecABCD-dependent homologous pairing."
Dixon D.A., Kowalczykowski S.C.
J. Biol. Chem. 270:16360-16370(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION.
[11]"The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a chi-regulated manner."
Anderson D.G., Kowalczykowski S.C.
Cell 90:77-86(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION WITH RECBCD.
[12]"The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins."
Spies M., Kowalczykowski S.C.
Mol. Cell 21:573-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RECB, SUBUNIT.
[13]"The structure of the E. coli recA protein monomer and polymer."
Story R.M., Weber I.T., Steitz T.A.
Nature 355:318-325(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.
[14]Erratum
Story R.M., Weber I.T., Steitz T.A.
Nature 355:567-567(1992)
[15]"Structure of the recA protein-ADP complex."
Story R.M., Steitz T.A.
Nature 355:374-376(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-353 IN COMPLEX WITH ATP.
[16]"The RecA hexamer is a structural homologue of ring helicases."
Yu X., Egelman E.H.
Nat. Struct. Biol. 4:101-104(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00328 Genomic DNA. Translation: CAA23618.1.
U00096 Genomic DNA. Translation: AAC75741.1.
AP009048 Genomic DNA. Translation: BAA16561.2.
PIRRQECA. G65049.
RefSeqNP_417179.1. NC_000913.3.
YP_490908.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A7G6.
SMRP0A7G6. Positions 7-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31832N.
IntActP0A7G6. 28 interactions.
MINTMINT-1300726.
STRING511145.b2699.

Chemistry

ChEMBLCHEMBL3434.

2D gel databases

SWISS-2DPAGEP0A7G6.

Proteomic databases

PaxDbP0A7G6.
PRIDEP0A7G6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75741; AAC75741; b2699.
BAA16561; BAA16561; BAA16561.
GeneID12930224.
947170.
KEGGecj:Y75_p2637.
eco:b2699.
PATRIC32120796. VBIEscCol129921_2790.

Organism-specific databases

EchoBASEEB0816.
EcoGeneEG10823. recA.

Phylogenomic databases

eggNOGCOG0468.
HOGENOMHOG000264120.
KOK03553.
OMAGNRVKAK.
OrthoDBEOG6ZKXNZ.
PhylomeDBP0A7G6.

Enzyme and pathway databases

BioCycEcoCyc:EG10823-MONOMER.
ECOL316407:JW2669-MONOMER.

Gene expression databases

GenevestigatorP0A7G6.

Family and domain databases

Gene3D3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_00268. RecA.
InterProIPR003593. 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]
PANTHERPTHR22942:SF1. PTHR22942:SF1. 1 hit.
PfamPF00154. RecA. 1 hit.
[Graphical view]
PRINTSPR00142. RECA.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
TIGRFAMsTIGR02012. tigrfam_recA. 1 hit.
PROSITEPS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7G6.
PROP0A7G6.

Entry information

Entry nameRECA_ECOLI
AccessionPrimary (citable) accession number: P0A7G6
Secondary accession number(s): P03017, P26347, P78213
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene