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P08394

- RECB_ECOLI

UniProt

P08394 - RECB_ECOLI

Protein

RecBCD enzyme subunit RecB

Gene

recB

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 131 (01 Oct 2014)
      Sequence version 1 (01 Aug 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 has ss- and dsDNA-dependent ATPase activity, exo- and endonuclease activity, 3'-5' helicase activity and loads RecA onto ssDNA. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions.16 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

    Cofactori

    Bind 1 Mg2+ per subunit Probable. Magnesium is required for both helicase and nuclease activity; its relative concentrations alter helicase speed and nuclease activity in a complicated fashion.3 PublicationsCuratedUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi956 – 9561Magnesium; via tele nitrogenCurated
    Metal bindingi1067 – 10671MagnesiumCurated
    Metal bindingi1080 – 10801MagnesiumCurated
    Metal bindingi1081 – 10811Magnesium; via carbonyl oxygenCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 308ATP
    DNA bindingi252 – 2543
    DNA bindingi511 – 5122
    DNA bindingi560 – 5612
    DNA bindingi761 – 7611

    GO - Molecular functioni

    1. ATP binding Source: EcoliWiki
    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. metal ion binding Source: UniProtKB-KW
    7. 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, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10824-MONOMER.
    ECOL316407:JW2788-MONOMER.
    MetaCyc:EG10824-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RecBCD enzyme subunit RecBUniRule annotation (EC:3.1.11.5UniRule annotation)
    Alternative name(s):
    Exodeoxyribonuclease V 135 kDa polypeptide
    Exodeoxyribonuclease V beta chain
    Exonuclease V subunit RecBUniRule annotation
    Short name:
    ExoV subunit RecBUniRule annotation
    Helicase/nuclease RecBCD subunit RecBUniRule annotation
    Gene namesi
    Name:recBUniRule annotation
    Synonyms:ior, rorA
    Ordered Locus Names:b2820, JW2788
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10824. recB.

    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
    Mutagenesisi29 – 291K → Q: Subunit loses ATPase and 3'-5' helicase activity, holoenzyme has 3-fold less helicase activity, 20-fold less processivity. 1 Publication
    Mutagenesisi807 – 8071T → I in recB-2109; absence of nuclease modification at chi sites. 1 Publication
    Mutagenesisi1067 – 10671D → A: Subunit loses nuclease activity. 1 Publication
    Mutagenesisi1080 – 10801D → A: Loss of holoenzyme nuclease activity, retains full helicase activity, does not recognize chi, no loading of RecA on ssDNA and no recombinational repair. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11801179RecBCD enzyme subunit RecBPRO_0000102046Add
    BLAST

    Proteomic databases

    PaxDbiP08394.
    PRIDEiP08394.

    Expressioni

    Gene expression databases

    GenevestigatoriP08394.

    Interactioni

    Subunit structurei

    Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. The C-terminus interacts with RecA. Interacts with YgbT (Cas1).8 Publications

    Protein-protein interaction databases

    DIPiDIP-540N.
    IntActiP08394. 19 interactions.
    MINTiMINT-1224378.
    STRINGi511145.b2820.

    Structurei

    Secondary structure

    1
    1180
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 123
    Beta strandi19 – 224
    Helixi29 – 4113
    Beta strandi45 – 495
    Helixi56 – 583
    Beta strandi59 – 646
    Helixi66 – 8823
    Helixi95 – 1039
    Helixi107 – 12014
    Helixi121 – 1233
    Beta strandi125 – 1284
    Helixi129 – 13911
    Helixi141 – 1444
    Helixi157 – 17216
    Helixi177 – 18610
    Helixi190 – 1978
    Turni198 – 2014
    Beta strandi202 – 2043
    Beta strandi207 – 2104
    Helixi218 – 23417
    Beta strandi249 – 2513
    Helixi255 – 2639
    Helixi283 – 2875
    Helixi312 – 3165
    Helixi324 – 34623
    Helixi351 – 36313
    Helixi367 – 37711
    Beta strandi379 – 3835
    Helixi386 – 3883
    Helixi391 – 40111
    Beta strandi408 – 4136
    Helixi415 – 4173
    Turni421 – 4244
    Helixi427 – 43610
    Beta strandi440 – 4423
    Helixi451 – 46212
    Beta strandi463 – 4664
    Helixi482 – 4843
    Beta strandi487 – 4915
    Beta strandi494 – 4963
    Beta strandi498 – 5036
    Helixi513 – 53422
    Beta strandi538 – 5425
    Beta strandi545 – 5484
    Helixi551 – 5533
    Beta strandi554 – 5607
    Helixi561 – 57212
    Turni573 – 5753
    Beta strandi578 – 5803
    Helixi587 – 5893
    Helixi592 – 60312
    Helixi609 – 6179
    Helixi619 – 6213
    Helixi625 – 6339
    Helixi635 – 65521
    Helixi657 – 66711
    Helixi670 – 6767
    Beta strandi677 – 6793
    Helixi680 – 69819
    Helixi704 – 71613
    Helixi732 – 7343
    Beta strandi735 – 7406
    Turni741 – 7444
    Beta strandi749 – 7546
    Turni755 – 7584
    Beta strandi767 – 7693
    Turni771 – 7733
    Beta strandi776 – 7816
    Helixi784 – 80623
    Beta strandi809 – 8179
    Helixi832 – 8354
    Helixi837 – 8426
    Helixi850 – 85910
    Beta strandi865 – 8695
    Beta strandi901 – 9066
    Beta strandi908 – 9103
    Helixi917 – 9204
    Helixi942 – 9443
    Helixi949 – 95810
    Beta strandi964 – 9663
    Helixi970 – 97910
    Helixi984 – 9863
    Helixi987 – 99812
    Beta strandi1002 – 10065
    Helixi1009 – 10113
    Helixi1014 – 10163
    Beta strandi1017 – 102711
    Helixi1033 – 104311
    Beta strandi1059 – 107416
    Beta strandi1079 – 10824
    Helixi1090 – 10923
    Helixi1095 – 110410
    Turni1105 – 11073
    Helixi1108 – 112518
    Beta strandi1126 – 11283
    Helixi1131 – 11344
    Beta strandi1139 – 11457
    Helixi1164 – 117310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W36X-ray3.10B/E1-1180[»]
    3K70X-ray3.59B/E1-1180[»]
    ProteinModelPortaliP08394.
    SMRiP08394. Positions 343-809.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08394.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 450449UvrD-like helicase ATP-bindingUniRule annotationAdd
    BLAST
    Domaini480 – 746267UvrD-like helicase C-terminalUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 927926ATPase, DNA-binding and helicase activity, interacts with RecCAdd
    BLAST
    Regioni928 – 1180253Nuclease activity, interacts with RecD and RecAAdd
    BLAST

    Domaini

    The N-terminal DNA-binding domain (residues 1-929) is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function; both are stimulated in the presence of RecC, suggesting this domain interacts with RecC. Holoenzyme reconstituted with this truncated RecB has no nuclease activity (PubMed:9448271).1 Publication
    The C-terminal domain (residues 928-1180) has weak ssDNA endonuclease activity as an isolated fragment (PubMed:9790841) (PubMed:10518611). RecD probably interacts with this domain. It interacts with RecA, facilitating its loading onto ssDNA. Interaction is decreased by ATP (PubMed:16483938).3 Publications

    Sequence similaritiesi

    Belongs to the helicase family. UvrD subfamily.UniRule annotation
    Contains 1 uvrD-like helicase ATP-binding domain.UniRule annotation
    Contains 1 uvrD-like helicase C-terminal domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1074.
    HOGENOMiHOG000258330.
    KOiK03582.
    OMAiHIGELLQ.
    OrthoDBiEOG6677M1.
    PhylomeDBiP08394.

    Family and domain databases

    Gene3Di3.40.50.300. 5 hits.
    3.90.320.10. 1 hit.
    HAMAPiMF_01485. RecB.
    InterProiIPR014017. DNA_helicase_UvrD-like_C.
    IPR000212. DNA_helicase_UvrD/REP.
    IPR004586. ExoDNase_V_bsu.
    IPR011604. Exonuc_phg/RecB_C.
    IPR027417. P-loop_NTPase.
    IPR011335. Restrct_endonuc-II-like.
    IPR014016. UvrD-like_ATP-bd.
    [Graphical view]
    PANTHERiPTHR11070. PTHR11070. 1 hit.
    PfamiPF00580. UvrD-helicase. 1 hit.
    PF13361. UvrD_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsiTIGR00609. recB. 1 hit.
    PROSITEiPS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08394-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDVAETLDP LRLPLQGERL IEASAGTGKT FTIAALYLRL LLGLGGSAAF     50
    PRPLTVEELL VVTFTEAATA ELRGRIRSNI HELRIACLRE TTDNPLYERL 100
    LEEIDDKAQA AQWLLLAERQ MDEAAVFTIH GFCQRMLNLN AFESGMLFEQ 150
    QLIEDESLLR YQACADFWRR HCYPLPREIA QVVFETWKGP QALLRDINRY 200
    LQGEAPVIKA PPPDDETLAS RHAQIVARID TVKQQWRDAV GELDALIESS 250
    GIDRRKFNRS NQAKWIDKIS AWAEEETNSY QLPESLEKFS QRFLEDRTKA 300
    GGETPRHPLF EAIDQLLAEP LSIRDLVITR ALAEIRETVA REKRRRGELG 350
    FDDMLSRLDS ALRSESGEVL AAAIRTRFPV AMIDEFQDTD PQQYRIFRRI 400
    WHHQPETALL LIGDPKQAIY AFRGADIFTY MKARSEVHAH YTLDTNWRSA 450
    PGMVNSVNKL FSQTDDAFMF REIPFIPVKS AGKNQALRFV FKGETQPAMK 500
    MWLMEGESCG VGDYQSTMAQ VCAAQIRDWL QAGQRGEALL MNGDDARPVR 550
    ASDISVLVRS RQEAAQVRDA LTLLEIPSVY LSNRDSVFET LEAQEMLWLL 600
    QAVMTPEREN TLRSALATSM MGLNALDIET LNNDEHAWDV VVEEFDGYRQ 650
    IWRKRGVMPM LRALMSARNI AENLLATAGG ERRLTDILHI SELLQEAGTQ 700
    LESEHALVRW LSQHILEPDS NASSQQMRLE SDKHLVQIVT IHKSKGLEYP 750
    LVWLPFITNF RVQEQAFYHD RHSFEAVLDL NAAPESVDLA EAERLAEDLR 800
    LLYVALTRSV WHCSLGVAPL VRRRGDKKGD TDVHQSALGR LLQKGEPQDA 850
    AGLRTCIEAL CDDDIAWQTA QTGDNQPWQV NDVSTAELNA KTLQRLPGDN 900
    WRVTSYSGLQ QRGHGIAQDL MPRLDVDAAG VASVVEEPTL TPHQFPRGAS 950
    PGTFLHSLFE DLDFTQPVDP NWVREKLELG GFESQWEPVL TEWITAVLQA 1000
    PLNETGVSLS QLSARNKQVE MEFYLPISEP LIASQLDTLI RQFDPLSAGC 1050
    PPLEFMQVRG MLKGFIDLVF RHEGRYYLLD YKSNWLGEDS SAYTQQAMAA 1100
    AMQAHRYDLQ YQLYTLALHR YLRHRIADYD YEHHFGGVIY LFLRGVDKEH 1150
    PQQGIYTTRP NAGLIALMDE MFAGMTLEEA 1180
    Length:1,180
    Mass (Da):133,959
    Last modified:August 1, 1988 - v1
    Checksum:iF9AC331808E8F281
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04581 Genomic DNA. Translation: CAA28250.1.
    AF179304 Genomic DNA. Translation: AAD56369.1.
    U29581 Genomic DNA. Translation: AAB40467.1.
    U00096 Genomic DNA. Translation: AAC75859.1.
    AP009048 Genomic DNA. Translation: BAE76889.1.
    X06227 Genomic DNA. Translation: CAA29577.1.
    X04582 Genomic DNA. Translation: CAA28252.1.
    PIRiA25532. NCECX5.
    RefSeqiNP_417297.1. NC_000913.3.
    YP_491025.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75859; AAC75859; b2820.
    BAE76889; BAE76889; BAE76889.
    GeneIDi12933313.
    947286.
    KEGGiecj:Y75_p2754.
    eco:b2820.
    PATRICi32121058. VBIEscCol129921_2918.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04581 Genomic DNA. Translation: CAA28250.1 .
    AF179304 Genomic DNA. Translation: AAD56369.1 .
    U29581 Genomic DNA. Translation: AAB40467.1 .
    U00096 Genomic DNA. Translation: AAC75859.1 .
    AP009048 Genomic DNA. Translation: BAE76889.1 .
    X06227 Genomic DNA. Translation: CAA29577.1 .
    X04582 Genomic DNA. Translation: CAA28252.1 .
    PIRi A25532. NCECX5.
    RefSeqi NP_417297.1. NC_000913.3.
    YP_491025.1. 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 B/E 1-1180 [» ]
    3K70 X-ray 3.59 B/E 1-1180 [» ]
    ProteinModelPortali P08394.
    SMRi P08394. Positions 343-809.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-540N.
    IntActi P08394. 19 interactions.
    MINTi MINT-1224378.
    STRINGi 511145.b2820.

    Chemistry

    ChEMBLi CHEMBL2095232.

    Proteomic databases

    PaxDbi P08394.
    PRIDEi P08394.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75859 ; AAC75859 ; b2820 .
    BAE76889 ; BAE76889 ; BAE76889 .
    GeneIDi 12933313.
    947286.
    KEGGi ecj:Y75_p2754.
    eco:b2820.
    PATRICi 32121058. VBIEscCol129921_2918.

    Organism-specific databases

    EchoBASEi EB0817.
    EcoGenei EG10824. recB.

    Phylogenomic databases

    eggNOGi COG1074.
    HOGENOMi HOG000258330.
    KOi K03582.
    OMAi HIGELLQ.
    OrthoDBi EOG6677M1.
    PhylomeDBi P08394.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10824-MONOMER.
    ECOL316407:JW2788-MONOMER.
    MetaCyc:EG10824-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P08394.
    PROi P08394.

    Gene expression databases

    Genevestigatori P08394.

    Family and domain databases

    Gene3Di 3.40.50.300. 5 hits.
    3.90.320.10. 1 hit.
    HAMAPi MF_01485. RecB.
    InterProi IPR014017. DNA_helicase_UvrD-like_C.
    IPR000212. DNA_helicase_UvrD/REP.
    IPR004586. ExoDNase_V_bsu.
    IPR011604. Exonuc_phg/RecB_C.
    IPR027417. P-loop_NTPase.
    IPR011335. Restrct_endonuc-II-like.
    IPR014016. UvrD-like_ATP-bd.
    [Graphical view ]
    PANTHERi PTHR11070. PTHR11070. 1 hit.
    Pfami PF00580. UvrD-helicase. 1 hit.
    PF13361. UvrD_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    SSF52980. SSF52980. 1 hit.
    TIGRFAMsi TIGR00609. recB. 1 hit.
    PROSITEi PS51198. UVRD_HELICASE_ATP_BIND. 1 hit.
    PS51217. UVRD_HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the Escherichia coli recB gene."
      Finch P.W., Storey A., Chapman K.E., Brown K., Hickson I.D., Emmerson P.T.
      Nucleic Acids Res. 14:8573-8582(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme."
      Arnold D.A., Kowalczykowski S.C.
      J. Biol. Chem. 275:12261-12265(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN RECA LOADING, MUTAGENESIS OF THR-807.
      Strain: V1000.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    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 1-11.
    6. "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: PROTEIN SEQUENCE OF 2-11, FUNCTION AS AN EXONUCLEASE; ENDONUCLEASE; HELICASE AND ATPASE, SUBUNIT.
    7. "Complete nucleotide sequence of recD, the structural gene for the alpha subunit of Exonuclease V of Escherichia coli."
      Finch P.W., Storey A., Brown K., Hickson I.D., Emmerson P.T.
      Nucleic Acids Res. 14:8583-8594(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1093-1180.
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. "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.
    16. "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.
    17. "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, DOMAIN, MUTAGENESIS OF ASP-1080.
    18. "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, INTERACTION WITH RECC, DOMAIN, DNA-BINDING.
    19. "Isolation and characterization of the C-terminal nuclease domain from the RecB protein of Escherichia coli."
      Zhang X.J., Julin D.A.
      Nucleic Acids Res. 27:4200-4207(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF ASP-1080.
    20. Cited for: FUNCTION AS A BIPOLAR HELICASE.
    21. "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, RATE, DNA-BINDING, MUTAGENESIS OF LYS-29.
    22. "The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA."
      Sun J.Z., Julin D.A., Hu J.S.
      Biochemistry 45:131-140(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A NUCLEASE, COFACTOR, MUTAGENESIS OF ASP-1067 AND ASP-1080.
    23. "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 RECA, SUBUNIT, DOMAIN.
    24. "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.
    25. Cited for: POSSIBLE FUNCTION IN ALTERNATIVE END-JOINING.
      Strain: K12 / TG1.
    26. Cited for: INTERACTION WITH YGBT.
      Strain: K12.
    27. "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, COFACTOR, SUBUNIT.
    28. "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, COFACTOR, SUBUNIT.
    29. "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 nameiRECB_ECOLI
    AccessioniPrimary (citable) accession number: P08394
    Secondary accession number(s): Q2MA17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 131 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