Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RecBCD enzyme subunit RecC

Gene

recC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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 (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination (PubMed:4562392, PubMed:4552016, PubMed:123277). In the holoenzyme this subunit almost certainly recognizes the wild-type Chi sequence, 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.18 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

Activity regulationi

After reacting with DNA bearing a Chi site the holoenzyme is disassembled and loses exonuclease activity, DNA unwinding and Chi-directed DNA cleavage; RecB remains complexed with ssDNA, which may prevent holoenzyme reassembly (PubMed:10197988). High levels of Mg2+ (13 mM MgCl2+) or incubation with DNase allow holoenyzme reassembly, suggesting it is DNA bound to RecB that prevents reassembly (PubMed:10197988).2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi9711
DNA bindingi10011
DNA bindingi1078 – 10814

GO - Molecular functioni

  • ATP binding Source: UniProtKB-UniRule
  • ATP-dependent DNA helicase activity Source: UniProtKB-UniRule
  • DNA binding Source: UniProtKB-UniRule
  • exodeoxyribonuclease V activity Source: EcoCyc

GO - Biological processi

  • clearance of foreign intracellular DNA Source: UniProtKB
  • DNA recombination Source: EcoCyc
  • double-strand break repair via homologous recombination Source: EcoCyc
  • response to radiation Source: EcoCyc

Keywordsi

Molecular functionDNA-binding, Exonuclease, Helicase, Hydrolase, Nuclease
Biological processDNA damage, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10825-MONOMER
MetaCyc:EG10825-MONOMER
BRENDAi3.1.11.5 2026

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10825 recC

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Decreased degradation of DNA with free ends that is unable to undergo homologous recombination, which can fortuitously lead to more efficient viral infection (PubMed:4562392, PubMed:123277). 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)DescriptionActionsGraphical viewLength
Mutagenesisi38Q → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi64L → A: Does not act at Chi. 1 Publication1
Mutagenesisi70W → A: Does not act at Chi. 1 Publication1
Mutagenesisi133D → A: Does not act at Chi. 1 Publication1
Mutagenesisi134L → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi136D → A: Does not act at Chi. 1 Publication1
Mutagenesisi137Q → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi142R → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi186R → A, C or H: Does not act at Chi. 1 Publication1
Mutagenesisi705D → A or H: Acts at variant Chi sequences. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2095232

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000871201 – 1122RecBCD enzyme subunit RecCAdd BLAST1122

Proteomic databases

PaxDbiP07648
PRIDEiP07648

Interactioni

Subunit structurei

Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with YgbT (Cas1) (PubMed:21219465).UniRule annotation7 Publications

Protein-protein interaction databases

BioGridi4261821, 369 interactors
ComplexPortaliCPX-2197 Exodeoxyribonuclease V complex
DIPiDIP-10650N
IntActiP07648, 3 interactors
MINTiP07648
STRINGi316385.ECDH10B_2992

Structurei

Secondary structure

11122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP07648
SMRiP07648
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07648

Family & Domainsi

Domaini

The holoenzyme may undergo conformational shifts upon DNA binding: the nuclease domain of RecB may swing away from the DNA exit tunnel in RecC. When Chi DNA binds to the RecC tunnel, the nuclease domain may then swing back to its original position (that seen in crystal structures), allowing it to nick the DNA 3' of the Chi site and then rotate to load RecA. At high Mg2+ the nuclease domain may swing back more frequently, explaining differences seen in assays performed at high Mg2+.1 Publication

Sequence similaritiesi

Belongs to the RecC family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DSY Bacteria
COG1330 LUCA
HOGENOMiHOG000258319
InParanoidiP07648
KOiK03583
PhylomeDBiP07648

Family and domain databases

Gene3Di1.10.10.160, 1 hit
HAMAPiMF_01486 RecC, 1 hit
InterProiView protein in InterPro
IPR013986 DExx_box_DNA_helicase_dom_sf
IPR027417 P-loop_NTPase
IPR006697 RecC
IPR011335 Restrct_endonuc-II-like
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)DescriptionActionsGraphical viewLength
Natural varianti647 – 655QERISQRFL → KNVSASVF in recC-1004; holoenzyme prefers an altered Chi over wild-type Chi sequence. Pseudorevertant of a frameshift mutation at aa 647. 9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000946938.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75861; AAC75861; b2822
BAE76891; BAE76891; BAE76891
GeneIDi947294
KEGGiecj:JW2790
eco:b2822
PATRICifig|1411691.4.peg.3914

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000946938.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W36X-ray3.10C/F1-1122[»]
3K70X-ray3.59C/F1-1122[»]
5LD2electron microscopy3.83C1-1122[»]
5MBVelectron microscopy3.80C1-1122[»]
ProteinModelPortaliP07648
SMRiP07648
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261821, 369 interactors
ComplexPortaliCPX-2197 Exodeoxyribonuclease V complex
DIPiDIP-10650N
IntActiP07648, 3 interactors
MINTiP07648
STRINGi316385.ECDH10B_2992

Chemistry databases

ChEMBLiCHEMBL2095232

Proteomic databases

PaxDbiP07648
PRIDEiP07648

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75861; AAC75861; b2822
BAE76891; BAE76891; BAE76891
GeneIDi947294
KEGGiecj:JW2790
eco:b2822
PATRICifig|1411691.4.peg.3914

Organism-specific databases

EchoBASEiEB0818
EcoGeneiEG10825 recC

Phylogenomic databases

eggNOGiENOG4105DSY Bacteria
COG1330 LUCA
HOGENOMiHOG000258319
InParanoidiP07648
KOiK03583
PhylomeDBiP07648

Enzyme and pathway databases

BioCyciEcoCyc:EG10825-MONOMER
MetaCyc:EG10825-MONOMER
BRENDAi3.1.11.5 2026

Miscellaneous databases

EvolutionaryTraceiP07648
PROiPR:P07648

Family and domain databases

Gene3Di1.10.10.160, 1 hit
HAMAPiMF_01486 RecC, 1 hit
InterProiView protein in InterPro
IPR013986 DExx_box_DNA_helicase_dom_sf
IPR027417 P-loop_NTPase
IPR006697 RecC
IPR011335 Restrct_endonuc-II-like
PIRSFiPIRSF000980 RecC, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF52980 SSF52980, 1 hit
TIGRFAMsiTIGR01450 recC, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRECC_ECOLI
AccessioniPrimary (citable) accession number: P07648
Secondary accession number(s): Q2MA15, Q9RNX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 7, 2018
This is version 154 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again