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P0A7G6

- RECA_ECOLI

UniProt

P0A7G6 - RECA_ECOLI

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Protein

Protein RecA

Gene

recA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 748ATP1 PublicationUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. damaged DNA binding Source: UniProtKB-HAMAP
  3. DNA-dependent ATPase activity Source: UniProtKB-HAMAP
  4. single-stranded DNA binding Source: EcoliWiki

GO - Biological processi

  1. cell motility Source: EcoliWiki
  2. cellular response to DNA damage stimulus Source: EcoliWiki
  3. DNA recombination Source: CACAO
  4. DNA repair Source: UniProtKB-HAMAP
  5. response to ionizing radiation Source: EcoCyc
  6. SOS response Source: CACAO
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
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10823. recA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 353352Protein RecAPRO_0000122703Add
BLAST

Proteomic databases

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.

Gene expression databases

GenevestigatoriP0A7G6.

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

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP0A7G6.
SMRiP0A7G6. Positions 7-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7G6.

Family & Domainsi

Sequence similaritiesi

Belongs to the RecA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0468.
HOGENOMiHOG000264120.
InParanoidiP0A7G6.
KOiK03553.
OMAiGNRVKAK.
OrthoDBiEOG6ZKXNZ.
PhylomeDBiP0A7G6.

Family and domain databases

Gene3Di3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00268. RecA.
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:
EMBL
GenBank
DDBJ
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.
YP_490908.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75741; AAC75741; b2699.
BAA16561; BAA16561; BAA16561.
GeneIDi12930224.
947170.
KEGGiecj:Y75_p2637.
eco:b2699.
PATRICi32120796. VBIEscCol129921_2790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00328 Genomic DNA. Translation: CAA23618.1 .
U00096 Genomic DNA. Translation: AAC75741.1 .
AP009048 Genomic DNA. Translation: BAA16561.2 .
PIRi G65049. RQECA.
RefSeqi NP_417179.1. NC_000913.3.
YP_490908.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AA3 NMR - A 269-331 [» ]
1N03 electron microscopy 20.00 A/B/C/D/E/F/G 2-353 [» ]
1REA X-ray 2.70 A 2-353 [» ]
1U94 X-ray 1.90 A 2-353 [» ]
1U98 X-ray 2.00 A 2-353 [» ]
1U99 X-ray 2.60 A 2-353 [» ]
1XMS X-ray 2.10 A 2-353 [» ]
1XMV X-ray 1.90 A 2-353 [» ]
2REB X-ray 2.30 A 2-353 [» ]
2REC electron microscopy - A/B/C/D/E/F 1-353 [» ]
3CMT X-ray 3.15 A/D 2-335 [» ]
3CMU X-ray 4.20 A 2-335 [» ]
3CMV X-ray 4.30 A/B/C/D/E/F/G/H 2-335 [» ]
3CMW X-ray 2.80 A/C 2-335 [» ]
3CMX X-ray 3.40 A/D 2-335 [» ]
ProteinModelPortali P0A7G6.
SMRi P0A7G6. Positions 7-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31832N.
IntActi P0A7G6. 28 interactions.
MINTi MINT-1300726.
STRINGi 511145.b2699.

Chemistry

ChEMBLi CHEMBL3434.

2D gel databases

SWISS-2DPAGE P0A7G6.

Proteomic databases

PaxDbi P0A7G6.
PRIDEi P0A7G6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75741 ; AAC75741 ; b2699 .
BAA16561 ; BAA16561 ; BAA16561 .
GeneIDi 12930224.
947170.
KEGGi ecj:Y75_p2637.
eco:b2699.
PATRICi 32120796. VBIEscCol129921_2790.

Organism-specific databases

EchoBASEi EB0816.
EcoGenei EG10823. recA.

Phylogenomic databases

eggNOGi COG0468.
HOGENOMi HOG000264120.
InParanoidi P0A7G6.
KOi K03553.
OMAi GNRVKAK.
OrthoDBi EOG6ZKXNZ.
PhylomeDBi P0A7G6.

Enzyme and pathway databases

BioCyci EcoCyc:EG10823-MONOMER.
ECOL316407:JW2669-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7G6.
PROi P0A7G6.

Gene expression databases

Genevestigatori P0A7G6.

Family and domain databases

Gene3Di 3.30.250.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_00268. RecA.
InterProi IPR003593. 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 ]
PANTHERi PTHR22942:SF1. PTHR22942:SF1. 1 hit.
Pfami PF00154. RecA. 1 hit.
[Graphical view ]
PRINTSi PR00142. RECA.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF54752. SSF54752. 1 hit.
TIGRFAMsi TIGR02012. tigrfam_recA. 1 hit.
PROSITEi PS00321. RECA_1. 1 hit.
PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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).

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: October 29, 2014
This is version 95 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

External Data

Dasty 3