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P07648

- RECC_ECOLI

UniProt

P07648 - RECC_ECOLI

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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

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

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, 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
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
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.
InParanoidiP07648.
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

        10         20         30         40         50
MLRVYHSNRL DVLEALMEFI VERERLDDPF EPEMILVQST GMAQWLQMTL
60 70 80 90 100
SQKFGIAANI DFPLPASFIW DMFVRVLPEI PKESAFNKQS MSWKLMTLLP
110 120 130 140 150
QLLEREDFTL LRHYLTDDSD KRKLFQLSSK AADLFDQYLV YRPDWLAQWE
160 170 180 190 200
TGHLVEGLGE AQAWQAPLWK ALVEYTHQLG QPRWHRANLY QRFIETLESA
210 220 230 240 250
TTCPPGLPSR VFICGISALP PVYLQALQAL GKHIEIHLLF TNPCRYYWGD
260 270 280 290 300
IKDPAYLAKL LTRQRRHSFE DRELPLFRDS ENAGQLFNSD GEQDVGNPLL
310 320 330 340 350
ASWGKLGRDY IYLLSDLESS QELDAFVDVT PDNLLHNIQS DILELENRAV
360 370 380 390 400
AGVNIEEFSR SDNKRPLDPL DSSITFHVCH SPQREVEVLH DRLLAMLEED
410 420 430 440 450
PTLTPRDIIV MVADIDSYSP FIQAVFGSAP ADRYLPYAIS DRRARQSHPV
460 470 480 490 500
LEAFISLLSL PDSRFVSEDV LALLDVPVLA ARFDITEEGL RYLRQWVNES
510 520 530 540 550
GIRWGIDDDN VRELELPATG QHTWRFGLTR MLLGYAMESA QGEWQSVLPY
560 570 580 590 600
DESSGLIAEL VGHLASLLMQ LNIWRRGLAQ ERPLEEWLPV CRDMLNAFFL
610 620 630 640 650
PDAETEAAMT LIEQQWQAII AEGLGAQYGD AVPLSLLRDE LAQRLDQERI
660 670 680 690 700
SQRFLAGPVN ICTLMPMRSI PFKVVCLLGM NDGVYPRQLA PLGFDLMSQK
710 720 730 740 750
PKRGDRSRRD DDRYLFLEAL ISAQQKLYIS YIGRSIQDNS ERFPSVLVQE
760 770 780 790 800
LIDYIGQSHY LPGDEALNCD ESEARVKAHL TCLHTRMPFD PQNYQPGERQ
810 820 830 840 850
SYAREWLPAA SQAGKAHSEF VQPLPFTLPE TVPLETLQRF WAHPVRAFFQ
860 870 880 890 900
MRLQVNFRTE DSEIPDTEPF ILEGLSRYQI NQQLLNALVE QDDAERLFRR
910 920 930 940 950
FRAAGDLPYG AFGEIFWETQ CQEMQQLADR VIACRQPGQS MEIDLACNGV
960 970 980 990 1000
QITGWLPQVQ PDGLLRWRPS LLSVAQGMQL WLEHLVYCAS GGNGESRLFL
1010 1020 1030 1040 1050
RKDGEWRFPP LAAEQALHYL SQLIEGYREG MSAPLLVLPE SGGAWLKTCY
1060 1070 1080 1090 1100
DAQNDAMLDD DSTLQKARTK FLQAYEGNMM VRGEGDDIWY QRLWRQLTPE
1110 1120
TMEAIVEQSQ RFLLPLFRFN QS
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.
InParanoidi P07648.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 123 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