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Protein

RecBCD enzyme subunit RecC

Gene

recC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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 (>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

Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi971 – 9711
DNA bindingi1001 – 10011
DNA bindingi1078 – 10814

GO - Molecular functioni

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

GO - Biological processi

  • clearance of foreign intracellular DNA Source: UniProtKB
  • DNA recombination Source: EcoCyc
  • double-strand break repair Source: EcoCyc
  • double-strand break repair via homologous recombination Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10825. recC.

Subcellular locationi

GO - Cellular componenti

  • exodeoxyribonuclease V complex Source: EcoCyc
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381Q → A: Acts at variant Chi sequences. 1 Publication
Mutagenesisi64 – 641L → A: Does not act at Chi. 1 Publication
Mutagenesisi70 – 701W → A: Does not act at Chi. 1 Publication
Mutagenesisi133 – 1331D → A: Does not act at Chi. 1 Publication
Mutagenesisi134 – 1341L → A: Acts at variant Chi sequences. 1 Publication
Mutagenesisi136 – 1361D → A: Does not act at Chi. 1 Publication
Mutagenesisi137 – 1371Q → A: Acts at variant Chi sequences. 1 Publication
Mutagenesisi142 – 1421R → A: Acts at variant Chi sequences. 1 Publication
Mutagenesisi186 – 1861R → A, C or H: Does not act at Chi. 1 Publication
Mutagenesisi705 – 7051D → A or H: Acts at variant Chi sequences. 1 Publication

Chemistry

ChEMBLiCHEMBL2095232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11221122RecBCD enzyme subunit RecCPRO_0000087120Add
BLAST

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 interactions.
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 – 87Combined sources
Helixi10 – 2213Combined sources
Beta strandi34 – 363Combined sources
Helixi40 – 5213Combined sources
Helixi65 – 7612Combined sources
Beta strandi77 – 793Combined sources
Helixi88 – 10215Combined sources
Beta strandi104 – 1063Combined sources
Helixi109 – 1146Combined sources
Helixi122 – 13817Combined sources
Helixi143 – 1508Combined sources
Helixi162 – 17817Combined sources
Turni187 – 1893Combined sources
Helixi190 – 1989Combined sources
Beta strandi209 – 2157Combined sources
Helixi221 – 23010Combined sources
Turni231 – 2333Combined sources
Beta strandi234 – 2418Combined sources
Helixi254 – 2574Combined sources
Turni258 – 2603Combined sources
Beta strandi264 – 2707Combined sources
Helixi279 – 2824Combined sources
Beta strandi288 – 2914Combined sources
Helixi298 – 3036Combined sources
Helixi305 – 31410Combined sources
Beta strandi318 – 3247Combined sources
Helixi334 – 34411Combined sources
Helixi355 – 3595Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi373 – 3819Combined sources
Helixi382 – 39918Combined sources
Helixi405 – 4073Combined sources
Beta strandi408 – 4136Combined sources
Helixi415 – 42511Combined sources
Beta strandi441 – 4433Combined sources
Helixi445 – 4473Combined sources
Helixi449 – 4579Combined sources
Helixi458 – 4625Combined sources
Helixi467 – 4737Combined sources
Helixi477 – 4826Combined sources
Helixi487 – 50014Combined sources
Helixi508 – 5136Combined sources
Beta strandi520 – 5234Combined sources
Helixi524 – 53512Combined sources
Beta strandi544 – 5463Combined sources
Helixi558 – 57720Combined sources
Helixi584 – 5874Combined sources
Helixi590 – 5989Combined sources
Helixi604 – 62522Combined sources
Helixi634 – 64714Combined sources
Turni652 – 6554Combined sources
Beta strandi656 – 6583Combined sources
Beta strandi660 – 6623Combined sources
Beta strandi672 – 6787Combined sources
Turni682 – 6843Combined sources
Helixi696 – 6994Combined sources
Helixi708 – 72215Combined sources
Beta strandi723 – 73210Combined sources
Beta strandi736 – 7383Combined sources
Helixi746 – 75611Combined sources
Beta strandi765 – 7673Combined sources
Helixi769 – 78012Combined sources
Helixi791 – 7933Combined sources
Beta strandi794 – 7974Combined sources
Helixi804 – 8063Combined sources
Helixi807 – 8104Combined sources
Helixi834 – 8407Combined sources
Beta strandi841 – 8433Combined sources
Helixi844 – 8507Combined sources
Turni851 – 8533Combined sources
Helixi874 – 88916Combined sources
Helixi894 – 90411Combined sources
Helixi910 – 93223Combined sources
Beta strandi939 – 9479Combined sources
Beta strandi950 – 95910Combined sources
Beta strandi961 – 9677Combined sources
Helixi974 – 98916Combined sources
Beta strandi995 – 9995Combined sources
Helixi1001 – 10033Combined sources
Beta strandi1005 – 10084Combined sources
Helixi1013 – 102917Combined sources
Turni1030 – 10323Combined sources
Helixi1039 – 104911Combined sources
Helixi1053 – 10553Combined sources
Helixi1061 – 107515Combined sources
Beta strandi1079 – 10813Combined sources
Helixi1088 – 10914Combined sources
Helixi1099 – 111719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

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.
OMAiSWMRRYP.
PhylomeDBiP07648.

Family and domain databases

Gene3Di1.10.10.160. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_01486. RecC. 1 hit.
InterProiIPR013986. DExx_box_DNA_helicase_dom.
IPR027417. P-loop_NTPase.
IPR006697. RecC.
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 frameshift mutation at aa 647.

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.
PATRICi32121062. VBIEscCol129921_2920.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1W36X-ray3.10C/F1-1122[»]
3K70X-ray3.59C/F1-1122[»]
ProteinModelPortaliP07648.
SMRiP07648. Positions 1-1121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261821. 369 interactions.
DIPiDIP-10650N.
IntActiP07648. 3 interactions.
MINTiMINT-1318941.
STRINGi511145.b2822.

Chemistry

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.
PATRICi32121062. VBIEscCol129921_2920.

Organism-specific databases

EchoBASEiEB0818.
EcoGeneiEG10825. recC.

Phylogenomic databases

eggNOGiENOG4105DSY. Bacteria.
COG1330. LUCA.
HOGENOMiHOG000258319.
InParanoidiP07648.
KOiK03583.
OMAiSWMRRYP.
PhylomeDBiP07648.

Enzyme and pathway databases

BioCyciEcoCyc:EG10825-MONOMER.
ECOL316407:JW2790-MONOMER.
MetaCyc:EG10825-MONOMER.
BRENDAi3.1.11.5. 2026.

Miscellaneous databases

EvolutionaryTraceiP07648.
PROiP07648.

Family and domain databases

Gene3Di1.10.10.160. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_01486. RecC. 1 hit.
InterProiIPR013986. DExx_box_DNA_helicase_dom.
IPR027417. P-loop_NTPase.
IPR006697. RecC.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 7, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.