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P08394

- RECB_ECOLI

UniProt

P08394 - RECB_ECOLI

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Protein
RecBCD enzyme subunit RecB
Gene
recB, ior, rorA, b2820, JW2788
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.17 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 Inferred. Magnesium is required for both helicase and nuclease activity; its relative concentrations alter helicase speed and nuclease activity in a complicated fashion.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi956 – 9561Magnesium; via tele nitrogen Inferred
Metal bindingi1067 – 10671Magnesium Inferred
Metal bindingi1080 – 10801Magnesium Inferred
Metal bindingi1081 – 10811Magnesium; via carbonyl oxygen Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 308ATPUniRule annotation
DNA bindingi252 – 25432 Publications
DNA bindingi511 – 51222 Publications
DNA bindingi560 – 56122 Publications
DNA bindingi761 – 76112 Publications

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
Complete GO annotation...

GO - Biological processi

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

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 RecB (EC:3.1.11.5)
Alternative name(s):
Exodeoxyribonuclease V 135 kDa polypeptide
Exodeoxyribonuclease V beta chain
Exonuclease V subunit RecB
Short name:
ExoV subunit RecB
Helicase/nuclease RecBCD subunit RecB
Gene namesi
Name:recB
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
Complete GO annotation...

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 RecBUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP08394.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 450449UvrD-like helicase ATP-binding
Add
BLAST
Domaini480 – 746267UvrD-like helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 927926ATPase, DNA-binding and helicase activity, interacts with RecCUniRule annotation
Add
BLAST
Regioni928 – 1180253Nuclease activity, interacts with RecD and RecAUniRule annotation
Add
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 (1 Publication).4 Publications
The C-terminal domain (residues 928-1180) has weak ssDNA endonuclease activity as an isolated fragment (1 Publication) (1 Publication). RecD probably interacts with this domain. It interacts with RecA, facilitating its loading onto ssDNA. Interaction is decreased by ATP (1 Publication).4 Publications

Sequence similaritiesi

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 130 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

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