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P07648

- RECC_ECOLI

UniProt

P07648 - RECC_ECOLI

Protein

RecBCD enzyme subunit RecC

Gene

recC

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 122 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid and highly processive ATP-dependent bidirectional helicase (1350 bp/s). Degrades the ssDNA until it encounters a chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts DNA near or within the chi site, attentuating 3'- but not 5'-exonuclease activity. The altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades foreign DNA, contributing to antiviral protection. It may also be involved in alternative end-joining, a modified version of non-homologous end-joining of DSBs. This subunit recognizes the wild-type chi sequence, and when added to isolated RecB increases its ATP-dependent helicase processivity. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions.14 Publications

    Catalytic activityi

    Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi971 – 9711
    DNA bindingi1001 – 10011
    DNA bindingi1078 – 10814

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: EcoCyc
    3. DNA binding Source: UniProtKB-KW
    4. endonuclease activity Source: EcoCyc
    5. exodeoxyribonuclease V activity Source: EcoCyc
    6. protein binding Source: EcoCyc

    GO - Biological processi

    1. clearance of foreign intracellular DNA Source: UniProtKB
    2. defense response to virus Source: UniProtKB-KW
    3. DNA catabolic process, exonucleolytic Source: GOC
    4. DNA duplex unwinding Source: GOC
    5. DNA recombination Source: EcoCyc
    6. double-strand break repair Source: EcoCyc
    7. nucleic acid phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease

    Keywords - Biological processi

    Antiviral defense, DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10825-MONOMER.
    ECOL316407:JW2790-MONOMER.
    MetaCyc:EG10825-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RecBCD enzyme subunit RecCUniRule annotation (EC:3.1.11.5UniRule annotation)
    Alternative name(s):
    Exodeoxyribonuclease V 125 kDa polypeptide
    Exodeoxyribonuclease V gamma chain
    Exonuclease V subunit RecCUniRule annotation
    Short name:
    ExoV subunit RecCUniRule annotation
    Gene namesi
    Name:recCUniRule annotation
    Ordered Locus Names:b2822, JW2790
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10825. recC.

    Subcellular locationi

    GO - Cellular componenti

    1. exodeoxyribonuclease V complex Source: EcoCyc

    Pathology & Biotechi

    Disruption phenotypei

    Decreased degradation of viral DNA with free ends, more efficient viral infection. Cells are deficient in DNA recombination repair and have increased sensitivity to UV light. The cultures have many inviable cells.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381Q → A: Recognizes variant chi sequences. 1 Publication
    Mutagenesisi64 – 641L → A: No recognition of chi. 1 Publication
    Mutagenesisi70 – 701W → A: No recognition of chi. 1 Publication
    Mutagenesisi133 – 1331D → A: No recognition of chi. 1 Publication
    Mutagenesisi134 – 1341L → A: Recognizes variant chi sequences. 1 Publication
    Mutagenesisi136 – 1361D → A: No recognition of chi. 1 Publication
    Mutagenesisi137 – 1371Q → A: Recognizes variant chi sequences. 1 Publication
    Mutagenesisi142 – 1421R → A: Recognizes variant chi sequences. 1 Publication
    Mutagenesisi186 – 1861R → A, C or H: No recognition of chi. 1 Publication
    Mutagenesisi705 – 7051D → A or H: Recognizes variant chi sequences. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11221122RecBCD enzyme subunit RecCPRO_0000087120Add
    BLAST

    Proteomic databases

    PaxDbiP07648.
    PRIDEiP07648.

    Expressioni

    Gene expression databases

    GenevestigatoriP07648.

    Interactioni

    Subunit structurei

    Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with YgbT (Cas1).7 PublicationsUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-10650N.
    IntActiP07648. 3 interactions.
    MINTiMINT-1318941.
    STRINGi511145.b2822.

    Structurei

    Secondary structure

    1
    1122
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87
    Helixi10 – 2213
    Beta strandi34 – 363
    Helixi40 – 5213
    Helixi65 – 7612
    Beta strandi77 – 793
    Helixi88 – 10215
    Beta strandi104 – 1063
    Helixi109 – 1146
    Helixi122 – 13817
    Helixi143 – 1508
    Helixi162 – 17817
    Turni187 – 1893
    Helixi190 – 1989
    Beta strandi209 – 2157
    Helixi221 – 23010
    Turni231 – 2333
    Beta strandi234 – 2418
    Helixi254 – 2574
    Turni258 – 2603
    Beta strandi264 – 2707
    Helixi279 – 2824
    Beta strandi288 – 2914
    Helixi298 – 3036
    Helixi305 – 31410
    Beta strandi318 – 3247
    Helixi334 – 34411
    Helixi355 – 3595
    Beta strandi364 – 3663
    Beta strandi373 – 3819
    Helixi382 – 39918
    Helixi405 – 4073
    Beta strandi408 – 4136
    Helixi415 – 42511
    Beta strandi441 – 4433
    Helixi445 – 4473
    Helixi449 – 4579
    Helixi458 – 4625
    Helixi467 – 4737
    Helixi477 – 4826
    Helixi487 – 50014
    Helixi508 – 5136
    Beta strandi520 – 5234
    Helixi524 – 53512
    Beta strandi544 – 5463
    Helixi558 – 57720
    Helixi584 – 5874
    Helixi590 – 5989
    Helixi604 – 62522
    Helixi634 – 64714
    Turni652 – 6554
    Beta strandi656 – 6583
    Beta strandi660 – 6623
    Beta strandi672 – 6787
    Turni682 – 6843
    Helixi696 – 6994
    Helixi708 – 72215
    Beta strandi723 – 73210
    Beta strandi736 – 7383
    Helixi746 – 75611
    Beta strandi765 – 7673
    Helixi769 – 78012
    Helixi791 – 7933
    Beta strandi794 – 7974
    Helixi804 – 8063
    Helixi807 – 8104
    Helixi834 – 8407
    Beta strandi841 – 8433
    Helixi844 – 8507
    Turni851 – 8533
    Helixi874 – 88916
    Helixi894 – 90411
    Helixi910 – 93223
    Beta strandi939 – 9479
    Beta strandi950 – 95910
    Beta strandi961 – 9677
    Helixi974 – 98916
    Beta strandi995 – 9995
    Helixi1001 – 10033
    Beta strandi1005 – 10084
    Helixi1013 – 102917
    Turni1030 – 10323
    Helixi1039 – 104911
    Helixi1053 – 10553
    Helixi1061 – 107515
    Beta strandi1079 – 10813
    Helixi1088 – 10914
    Helixi1099 – 111719

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W36X-ray3.10C/F1-1122[»]
    3K70X-ray3.59C/F1-1122[»]
    ProteinModelPortaliP07648.
    SMRiP07648. Positions 1-1121.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07648.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RecC family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1330.
    HOGENOMiHOG000258319.
    KOiK03583.
    OMAiDIVADKD.
    OrthoDBiEOG61P6M4.
    PhylomeDBiP07648.

    Family and domain databases

    Gene3Di1.10.10.160. 1 hit.
    3.40.50.300. 2 hits.
    HAMAPiMF_01486. RecC.
    InterProiIPR013986. DExx_box_DNA_helicase_dom.
    IPR006697. ExoDNase_V_gsu.
    IPR027417. P-loop_NTPase.
    IPR011335. Restrct_endonuc-II-like.
    [Graphical view]
    PIRSFiPIRSF000980. RecC. 1 hit.
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsiTIGR01450. recC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P07648-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRVYHSNRL DVLEALMEFI VERERLDDPF EPEMILVQST GMAQWLQMTL     50
    SQKFGIAANI DFPLPASFIW DMFVRVLPEI PKESAFNKQS MSWKLMTLLP 100
    QLLEREDFTL LRHYLTDDSD KRKLFQLSSK AADLFDQYLV YRPDWLAQWE 150
    TGHLVEGLGE AQAWQAPLWK ALVEYTHQLG QPRWHRANLY QRFIETLESA 200
    TTCPPGLPSR VFICGISALP PVYLQALQAL GKHIEIHLLF TNPCRYYWGD 250
    IKDPAYLAKL LTRQRRHSFE DRELPLFRDS ENAGQLFNSD GEQDVGNPLL 300
    ASWGKLGRDY IYLLSDLESS QELDAFVDVT PDNLLHNIQS DILELENRAV 350
    AGVNIEEFSR SDNKRPLDPL DSSITFHVCH SPQREVEVLH DRLLAMLEED 400
    PTLTPRDIIV MVADIDSYSP FIQAVFGSAP ADRYLPYAIS DRRARQSHPV 450
    LEAFISLLSL PDSRFVSEDV LALLDVPVLA ARFDITEEGL RYLRQWVNES 500
    GIRWGIDDDN VRELELPATG QHTWRFGLTR MLLGYAMESA QGEWQSVLPY 550
    DESSGLIAEL VGHLASLLMQ LNIWRRGLAQ ERPLEEWLPV CRDMLNAFFL 600
    PDAETEAAMT LIEQQWQAII AEGLGAQYGD AVPLSLLRDE LAQRLDQERI 650
    SQRFLAGPVN ICTLMPMRSI PFKVVCLLGM NDGVYPRQLA PLGFDLMSQK 700
    PKRGDRSRRD DDRYLFLEAL ISAQQKLYIS YIGRSIQDNS ERFPSVLVQE 750
    LIDYIGQSHY LPGDEALNCD ESEARVKAHL TCLHTRMPFD PQNYQPGERQ 800
    SYAREWLPAA SQAGKAHSEF VQPLPFTLPE TVPLETLQRF WAHPVRAFFQ 850
    MRLQVNFRTE DSEIPDTEPF ILEGLSRYQI NQQLLNALVE QDDAERLFRR 900
    FRAAGDLPYG AFGEIFWETQ CQEMQQLADR VIACRQPGQS MEIDLACNGV 950
    QITGWLPQVQ PDGLLRWRPS LLSVAQGMQL WLEHLVYCAS GGNGESRLFL 1000
    RKDGEWRFPP LAAEQALHYL SQLIEGYREG MSAPLLVLPE SGGAWLKTCY 1050
    DAQNDAMLDD DSTLQKARTK FLQAYEGNMM VRGEGDDIWY QRLWRQLTPE 1100
    TMEAIVEQSQ RFLLPLFRFN QS 1122
    Length:1,122
    Mass (Da):128,848
    Last modified:April 1, 1988 - v1
    Checksum:i48B90092DFC1BD21
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti647 – 6559QERISQRFL → KNVSASVF in recC-1004; holoenzyme prefers an altered chi over wild-type chi sequence. Pseudorevertant of a protein truncated at aa 663.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03966 Genomic DNA. Translation: CAA27604.1.
    U29581 Genomic DNA. Translation: AAB40469.1.
    U00096 Genomic DNA. Translation: AAC75861.1.
    AP009048 Genomic DNA. Translation: BAE76891.1.
    AF176618 Genomic DNA. Translation: AAD54314.1.
    X06227 Genomic DNA. Translation: CAA29575.1.
    PIRiA24137. NCECXV.
    RefSeqiNP_417299.1. NC_000913.3.
    YP_491027.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75861; AAC75861; b2822.
    BAE76891; BAE76891; BAE76891.
    GeneIDi12932827.
    947294.
    KEGGiecj:Y75_p2756.
    eco:b2822.
    PATRICi32121062. VBIEscCol129921_2920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03966 Genomic DNA. Translation: CAA27604.1 .
    U29581 Genomic DNA. Translation: AAB40469.1 .
    U00096 Genomic DNA. Translation: AAC75861.1 .
    AP009048 Genomic DNA. Translation: BAE76891.1 .
    AF176618 Genomic DNA. Translation: AAD54314.1 .
    X06227 Genomic DNA. Translation: CAA29575.1 .
    PIRi A24137. NCECXV.
    RefSeqi NP_417299.1. NC_000913.3.
    YP_491027.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W36 X-ray 3.10 C/F 1-1122 [» ]
    3K70 X-ray 3.59 C/F 1-1122 [» ]
    ProteinModelPortali P07648.
    SMRi P07648. Positions 1-1121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10650N.
    IntActi P07648. 3 interactions.
    MINTi MINT-1318941.
    STRINGi 511145.b2822.

    Chemistry

    ChEMBLi CHEMBL2095232.

    Proteomic databases

    PaxDbi P07648.
    PRIDEi P07648.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75861 ; AAC75861 ; b2822 .
    BAE76891 ; BAE76891 ; BAE76891 .
    GeneIDi 12932827.
    947294.
    KEGGi ecj:Y75_p2756.
    eco:b2822.
    PATRICi 32121062. VBIEscCol129921_2920.

    Organism-specific databases

    EchoBASEi EB0818.
    EcoGenei EG10825. recC.

    Phylogenomic databases

    eggNOGi COG1330.
    HOGENOMi HOG000258319.
    KOi K03583.
    OMAi DIVADKD.
    OrthoDBi EOG61P6M4.
    PhylomeDBi P07648.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10825-MONOMER.
    ECOL316407:JW2790-MONOMER.
    MetaCyc:EG10825-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P07648.
    PROi P07648.

    Gene expression databases

    Genevestigatori P07648.

    Family and domain databases

    Gene3Di 1.10.10.160. 1 hit.
    3.40.50.300. 2 hits.
    HAMAPi MF_01486. RecC.
    InterProi IPR013986. DExx_box_DNA_helicase_dom.
    IPR006697. ExoDNase_V_gsu.
    IPR027417. P-loop_NTPase.
    IPR011335. Restrct_endonuc-II-like.
    [Graphical view ]
    PIRSFi PIRSF000980. RecC. 1 hit.
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsi TIGR01450. recC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the Escherichia coli recC gene and of the thyA-recC intergenic region."
      Finch P.W., Wilson R.E., Brown K., Hickson I.D., Tomkinson A.E., Emmerson P.T.
      Nucleic Acids Res. 14:4437-4451(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "A novel, 11 nucleotide variant of chi, chi*: one of a class of sequences defining the Escherichia coli recombination hotspot chi."
      Arnold D.A., Handa N., Kobayashi I., Kowalczykowski S.C.
      J. Mol. Biol. 300:469-479(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RECC-1004 647-GLN--LEU-655, FUNCTION IN RECOGNITION OF CHI.
    5. "Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III."
      Finch P.W., Wilson R.E., Brown K., Hickson I.D., Emmerson P.T.
      Nucleic Acids Res. 14:7695-7703(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1114-1122.
    6. "Degradation of bacteriophage lambda deoxyribonucleic acid after restriction by Escherichia coli K-12."
      Simmon V.F., Lederberg S.
      J. Bacteriol. 112:161-169(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEGRADATION OF LAMBDA VIRUS DNA, DISRUPTION PHENOTYPE.
      Strain: K12.
    7. "Purification and properties of the recBC DNase of Escherichia coli K-12."
      Goldmark P.J., Linn S.
      J. Biol. Chem. 247:1849-1860(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ENDO- AND EXODEOXYRIBONUCLEASE, ATP-DEPENDENCE, SUBUNIT.
      Strain: K12.
    8. "The recBC deoxyribonuclease of Escherichia coli K-12. Substrate specificity and reaction intermediates."
      Karu A.E., MacKay V., Goldmark P.J., Linn S.
      J. Biol. Chem. 248:4874-4884(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATES, PROCESSIVITY.
    9. "Transfection of Escherichia coli spheroplasts. V. Activity of recBC nuclease in rec+ and rec minus spheroplasts measured with different forms of bacteriophage DNA."
      Benzinger R., Enquist L.W., Skalka A.
      J. Virol. 15:861-871(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEGRADATION OF VIRUS DNA, DISRUPTION PHENOTYPE.
    10. "Escherichia coli recBC deletion mutants."
      Chaudhury A.M., Smith G.R.
      J. Bacteriol. 160:788-791(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    11. "recD: the gene for an essential third subunit of exonuclease V."
      Amundsen S.K., Taylor A.F., Chaudhury A.M., Smith G.R.
      Proc. Natl. Acad. Sci. U.S.A. 83:5558-5562(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: OPERON, SUBUNIT.
    12. "Reconstitution of the activities of the RecBCD holoenzyme of Escherichia coli from the purified subunits."
      Masterson C., Boehmer P.E., McDonald F., Chaudhuri S., Hickson I.D., Emmerson P.T.
      J. Biol. Chem. 267:13564-13572(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN EXONUCLEASE; ENDONUCLEASE; HELICASE AND ATPASE, SUBUNIT.
    13. "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.
    14. "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 IN RECA-LOADING.
    15. "The recombination hotspot Chi is recognized by the translocating RecBCD enzyme as the single strand of DNA containing the sequence 5'-GCTGGTGG-3'."
      Bianco P.R., Kowalczykowski S.C.
      Proc. Natl. Acad. Sci. U.S.A. 94:6706-6711(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECOGNITION OF CHI.
    16. "Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme."
      Yu M., Souaya J., Julin D.A.
      J. Mol. Biol. 283:797-808(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROCESSIVITY.
    17. "The 30-kDa C-terminal domain of the RecB protein is critical for the nuclease activity, but not the helicase activity, of the RecBCD enzyme from Escherichia coli."
      Yu M., Souaya J., Julin D.A.
      Proc. Natl. Acad. Sci. U.S.A. 95:981-986(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROCESSIVITY, INTERACTION WITH RECB.
    18. Cited for: FUNCTION AS A BIPOLAR HELICASE.
    19. "Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme."
      Dillingham M.S., Webb M.R., Kowalczykowski S.C.
      J. Biol. Chem. 280:37069-37077(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor."
      Wu C.G., Bradford C., Lohman T.M.
      Nat. Struct. Mol. Biol. 17:1210-1217(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DUAL DIRECTION TRANSLOCATION.
    21. Cited for: POSSIBLE FUNCTION IN ALTERNATIVE END-JOINING.
      Strain: K12 / TG1.
    22. Cited for: INTERACTION WITH YGBT.
      Strain: K12.
    23. "Molecular determinants responsible for recognition of the single-stranded DNA regulatory sequence, chi, by RecBCD enzyme."
      Handa N., Yang L., Dillingham M.S., Kobayashi I., Wigley D.B., Kowalczykowski S.C.
      Proc. Natl. Acad. Sci. U.S.A. 109:8901-8906(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, MUTAGENESIS OF GLN-38; LEU-64; TRP-70; ASP-133; LEU-134; ASP-136; GLN-137; ARG-142; ARG-186 AND ASP-705.
    24. "Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks."
      Singleton M.R., Dillingham M.S., Gaudier M., Kowalczykowski S.C., Wigley D.B.
      Nature 432:187-193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH DNA, SUBUNIT.
    25. "DNA binding to RecD: role of the 1B domain in SF1B helicase activity."
      Saikrishnan K., Griffiths S.P., Cook N., Court R., Wigley D.B.
      EMBO J. 27:2222-2229(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) IN COMPLEX WITH DNA, SUBUNIT.
    26. "RecBCD enzyme and the repair of double-stranded DNA breaks."
      Dillingham M.S., Kowalczykowski S.C.
      Microbiol. Mol. Biol. Rev. 72:642-671(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiRECC_ECOLI
    AccessioniPrimary (citable) accession number: P07648
    Secondary accession number(s): Q2MA15, Q9RNX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 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