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P08394

- RECB_ECOLI

UniProt

P08394 - RECB_ECOLI

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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

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

Mg2+3 PublicationsCuratedUniRule annotationNote: Bind 1 Mg(2+) per subunit. 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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP08394.
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

        10         20         30         40         50
MSDVAETLDP LRLPLQGERL IEASAGTGKT FTIAALYLRL LLGLGGSAAF
60 70 80 90 100
PRPLTVEELL VVTFTEAATA ELRGRIRSNI HELRIACLRE TTDNPLYERL
110 120 130 140 150
LEEIDDKAQA AQWLLLAERQ MDEAAVFTIH GFCQRMLNLN AFESGMLFEQ
160 170 180 190 200
QLIEDESLLR YQACADFWRR HCYPLPREIA QVVFETWKGP QALLRDINRY
210 220 230 240 250
LQGEAPVIKA PPPDDETLAS RHAQIVARID TVKQQWRDAV GELDALIESS
260 270 280 290 300
GIDRRKFNRS NQAKWIDKIS AWAEEETNSY QLPESLEKFS QRFLEDRTKA
310 320 330 340 350
GGETPRHPLF EAIDQLLAEP LSIRDLVITR ALAEIRETVA REKRRRGELG
360 370 380 390 400
FDDMLSRLDS ALRSESGEVL AAAIRTRFPV AMIDEFQDTD PQQYRIFRRI
410 420 430 440 450
WHHQPETALL LIGDPKQAIY AFRGADIFTY MKARSEVHAH YTLDTNWRSA
460 470 480 490 500
PGMVNSVNKL FSQTDDAFMF REIPFIPVKS AGKNQALRFV FKGETQPAMK
510 520 530 540 550
MWLMEGESCG VGDYQSTMAQ VCAAQIRDWL QAGQRGEALL MNGDDARPVR
560 570 580 590 600
ASDISVLVRS RQEAAQVRDA LTLLEIPSVY LSNRDSVFET LEAQEMLWLL
610 620 630 640 650
QAVMTPEREN TLRSALATSM MGLNALDIET LNNDEHAWDV VVEEFDGYRQ
660 670 680 690 700
IWRKRGVMPM LRALMSARNI AENLLATAGG ERRLTDILHI SELLQEAGTQ
710 720 730 740 750
LESEHALVRW LSQHILEPDS NASSQQMRLE SDKHLVQIVT IHKSKGLEYP
760 770 780 790 800
LVWLPFITNF RVQEQAFYHD RHSFEAVLDL NAAPESVDLA EAERLAEDLR
810 820 830 840 850
LLYVALTRSV WHCSLGVAPL VRRRGDKKGD TDVHQSALGR LLQKGEPQDA
860 870 880 890 900
AGLRTCIEAL CDDDIAWQTA QTGDNQPWQV NDVSTAELNA KTLQRLPGDN
910 920 930 940 950
WRVTSYSGLQ QRGHGIAQDL MPRLDVDAAG VASVVEEPTL TPHQFPRGAS
960 970 980 990 1000
PGTFLHSLFE DLDFTQPVDP NWVREKLELG GFESQWEPVL TEWITAVLQA
1010 1020 1030 1040 1050
PLNETGVSLS QLSARNKQVE MEFYLPISEP LIASQLDTLI RQFDPLSAGC
1060 1070 1080 1090 1100
PPLEFMQVRG MLKGFIDLVF RHEGRYYLLD YKSNWLGEDS SAYTQQAMAA
1110 1120 1130 1140 1150
AMQAHRYDLQ YQLYTLALHR YLRHRIADYD YEHHFGGVIY LFLRGVDKEH
1160 1170 1180
PQQGIYTTRP NAGLIALMDE MFAGMTLEEA
Length:1,180
Mass (Da):133,959
Last modified:August 1, 1988 - v1
Checksum:iF9AC331808E8F281
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P08394.
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: November 26, 2014
This is version 133 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