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P0A7G6

- RECA_ECOLI

UniProt

P0A7G6 - RECA_ECOLI

Protein

Protein RecA

Gene

recA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: IntAct
    5. 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

    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-SubCell

    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.
    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

    MAIDENKQKA LAAALGQIEK QFGKGSIMRL GEDRSMDVET ISTGSLSLDI    50
    ALGAGGLPMG RIVEIYGPES SGKTTLTLQV IAAAQREGKT CAFIDAEHAL 100
    DPIYARKLGV DIDNLLCSQP DTGEQALEIC DALARSGAVD VIVVDSVAAL 150
    TPKAEIEGEI GDSHMGLAAR MMSQAMRKLA GNLKQSNTLL IFINQIRMKI 200
    GVMFGNPETT TGGNALKFYA SVRLDIRRIG AVKEGENVVG SETRVKVVKN 250
    KIAAPFKQAE FQILYGEGIN FYGELVDLGV KEKLIEKAGA WYSYKGEKIG 300
    QGKANATAWL KDNPETAKEI EKKVRELLLS NPNSTPDFSV DDSEGVAETN 350
    EDF 353
    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.
    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

    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 1, 2014
    This is version 94 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