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P07648 (RECC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RecBCD enzyme subunit RecC

EC=3.1.11.5
Alternative name(s):
Exodeoxyribonuclease V 125 kDa polypeptide
Exodeoxyribonuclease V gamma chain
Exonuclease V subunit RecC
Short name=ExoV subunit RecC
Gene names
Name:recC
Ordered Locus Names:b2822, JW2790
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Catalytic activity

Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides. HAMAP-Rule MF_01486

Subunit structure

Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with YgbT (Cas1). Ref.7 Ref.11 Ref.12 Ref.17 Ref.22 Ref.24 Ref.25

Disruption phenotype

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. Ref.6 Ref.9 Ref.10

Sequence similarities

Belongs to the RecC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11221122RecBCD enzyme subunit RecC HAMAP-Rule MF_01486
PRO_0000087120

Regions

DNA binding9711 Ref.23
DNA binding10011 Ref.23
DNA binding1078 – 10814 Ref.23

Natural variations

Natural variant647 – 6559QERISQRFL → KNVSASVF in recC-1004; holoenzyme prefers an altered chi over wild-type chi sequence. Pseudorevertant of a protein truncated at aa 663.

Experimental info

Mutagenesis381Q → A: Recognizes variant chi sequences. Ref.23
Mutagenesis641L → A: No recognition of chi. Ref.23
Mutagenesis701W → A: No recognition of chi. Ref.23
Mutagenesis1331D → A: No recognition of chi. Ref.23
Mutagenesis1341L → A: Recognizes variant chi sequences. Ref.23
Mutagenesis1361D → A: No recognition of chi. Ref.23
Mutagenesis1371Q → A: Recognizes variant chi sequences. Ref.23
Mutagenesis1421R → A: Recognizes variant chi sequences. Ref.23
Mutagenesis1861R → A, C or H: No recognition of chi. Ref.23
Mutagenesis7051D → A or H: Recognizes variant chi sequences. Ref.23

Secondary structure

................................................................................................................................................................ 1122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07648 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 48B90092DFC1BD21

FASTA1,122128,848
        10         20         30         40         50         60 
MLRVYHSNRL DVLEALMEFI VERERLDDPF EPEMILVQST GMAQWLQMTL SQKFGIAANI 

        70         80         90        100        110        120 
DFPLPASFIW DMFVRVLPEI PKESAFNKQS MSWKLMTLLP QLLEREDFTL LRHYLTDDSD 

       130        140        150        160        170        180 
KRKLFQLSSK AADLFDQYLV YRPDWLAQWE TGHLVEGLGE AQAWQAPLWK ALVEYTHQLG 

       190        200        210        220        230        240 
QPRWHRANLY QRFIETLESA TTCPPGLPSR VFICGISALP PVYLQALQAL GKHIEIHLLF 

       250        260        270        280        290        300 
TNPCRYYWGD IKDPAYLAKL LTRQRRHSFE DRELPLFRDS ENAGQLFNSD GEQDVGNPLL 

       310        320        330        340        350        360 
ASWGKLGRDY IYLLSDLESS QELDAFVDVT PDNLLHNIQS DILELENRAV AGVNIEEFSR 

       370        380        390        400        410        420 
SDNKRPLDPL DSSITFHVCH SPQREVEVLH DRLLAMLEED PTLTPRDIIV MVADIDSYSP 

       430        440        450        460        470        480 
FIQAVFGSAP ADRYLPYAIS DRRARQSHPV LEAFISLLSL PDSRFVSEDV LALLDVPVLA 

       490        500        510        520        530        540 
ARFDITEEGL RYLRQWVNES GIRWGIDDDN VRELELPATG QHTWRFGLTR MLLGYAMESA 

       550        560        570        580        590        600 
QGEWQSVLPY DESSGLIAEL VGHLASLLMQ LNIWRRGLAQ ERPLEEWLPV CRDMLNAFFL 

       610        620        630        640        650        660 
PDAETEAAMT LIEQQWQAII AEGLGAQYGD AVPLSLLRDE LAQRLDQERI SQRFLAGPVN 

       670        680        690        700        710        720 
ICTLMPMRSI PFKVVCLLGM NDGVYPRQLA PLGFDLMSQK PKRGDRSRRD DDRYLFLEAL 

       730        740        750        760        770        780 
ISAQQKLYIS YIGRSIQDNS ERFPSVLVQE LIDYIGQSHY LPGDEALNCD ESEARVKAHL 

       790        800        810        820        830        840 
TCLHTRMPFD PQNYQPGERQ SYAREWLPAA SQAGKAHSEF VQPLPFTLPE TVPLETLQRF 

       850        860        870        880        890        900 
WAHPVRAFFQ MRLQVNFRTE DSEIPDTEPF ILEGLSRYQI NQQLLNALVE QDDAERLFRR 

       910        920        930        940        950        960 
FRAAGDLPYG AFGEIFWETQ CQEMQQLADR VIACRQPGQS MEIDLACNGV QITGWLPQVQ 

       970        980        990       1000       1010       1020 
PDGLLRWRPS LLSVAQGMQL WLEHLVYCAS GGNGESRLFL RKDGEWRFPP LAAEQALHYL 

      1030       1040       1050       1060       1070       1080 
SQLIEGYREG MSAPLLVLPE SGGAWLKTCY DAQNDAMLDD DSTLQKARTK FLQAYEGNMM 

      1090       1100       1110       1120 
VRGEGDDIWY QRLWRQLTPE TMEAIVEQSQ RFLLPLFRFN QS 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"RecBCD enzyme is a bipolar DNA helicase."
Dillingham M.S., Spies M., Kowalczykowski S.C.
Nature 423:893-897(2003) [PubMed] [Europe PMC] [Abstract]
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]"An end-joining repair mechanism in Escherichia coli."
Chayot R., Montagne B., Mazel D., Ricchetti M.
Proc. Natl. Acad. Sci. U.S.A. 107:2141-2146(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION IN ALTERNATIVE END-JOINING.
Strain: K12 / TG1.
[22]"A dual function of the CRISPR-Cas system in bacterial antivirus immunity and DNA repair."
Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B., Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S., Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J., Edwards A.M., Yakunin A.F.
Mol. Microbiol. 79:484-502(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRNCECXV. A24137.
RefSeqNP_417299.1. NC_000913.3.
YP_491027.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W36X-ray3.10C/F1-1122[»]
3K70X-ray3.59C/F1-1122[»]
ProteinModelPortalP07648.
SMRP07648. Positions 1-1121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10650N.
IntActP07648. 3 interactions.
MINTMINT-1318941.
STRING511145.b2822.

Chemistry

ChEMBLCHEMBL2095232.

Proteomic databases

PaxDbP07648.
PRIDEP07648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75861; AAC75861; b2822.
BAE76891; BAE76891; BAE76891.
GeneID12932827.
947294.
KEGGecj:Y75_p2756.
eco:b2822.
PATRIC32121062. VBIEscCol129921_2920.

Organism-specific databases

EchoBASEEB0818.
EcoGeneEG10825. recC.

Phylogenomic databases

eggNOGCOG1330.
HOGENOMHOG000258319.
KOK03583.
OMADIVADKD.
OrthoDBEOG61P6M4.
PhylomeDBP07648.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP07648.

Family and domain databases

Gene3D1.10.10.160. 1 hit.
3.40.50.300. 2 hits.
HAMAPMF_01486. RecC.
InterProIPR013986. DExx_box_DNA_helicase_dom.
IPR006697. ExoDNase_V_gsu.
IPR027417. P-loop_NTPase.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PIRSFPIRSF000980. RecC. 1 hit.
SUPFAMSSF52540. SSF52540. 2 hits.
SSF52980. SSF52980. 1 hit.
TIGRFAMsTIGR01450. recC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP07648.
PROP07648.

Entry information

Entry nameRECC_ECOLI
AccessionPrimary (citable) accession number: P07648
Secondary accession number(s): Q2MA15, Q9RNX9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene