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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)DescriptionActionsGraphical viewLength
DNA bindingi9711
DNA bindingi10011
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)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.
DIPiDIP-10650N.
IntActiP07648. 3 interactors.
MINTiMINT-1318941.
STRINGi511145.b2822.

Structurei

Secondary structure

11122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi10 – 22Combined sources13
Beta strandi34 – 36Combined sources3
Helixi40 – 52Combined sources13
Helixi65 – 76Combined sources12
Beta strandi77 – 79Combined sources3
Helixi88 – 102Combined sources15
Beta strandi104 – 106Combined sources3
Helixi109 – 114Combined sources6
Helixi122 – 138Combined sources17
Helixi143 – 150Combined sources8
Helixi162 – 178Combined sources17
Turni187 – 189Combined sources3
Helixi190 – 198Combined sources9
Beta strandi209 – 215Combined sources7
Helixi221 – 230Combined sources10
Turni231 – 233Combined sources3
Beta strandi234 – 241Combined sources8
Helixi254 – 257Combined sources4
Turni258 – 260Combined sources3
Beta strandi264 – 270Combined sources7
Helixi279 – 282Combined sources4
Beta strandi288 – 291Combined sources4
Helixi298 – 303Combined sources6
Helixi305 – 314Combined sources10
Beta strandi318 – 324Combined sources7
Helixi334 – 344Combined sources11
Helixi355 – 359Combined sources5
Beta strandi364 – 366Combined sources3
Beta strandi373 – 381Combined sources9
Helixi382 – 399Combined sources18
Helixi405 – 407Combined sources3
Beta strandi408 – 413Combined sources6
Helixi415 – 425Combined sources11
Beta strandi441 – 443Combined sources3
Helixi445 – 447Combined sources3
Helixi449 – 457Combined sources9
Helixi458 – 462Combined sources5
Helixi467 – 473Combined sources7
Helixi477 – 482Combined sources6
Helixi487 – 500Combined sources14
Helixi508 – 513Combined sources6
Beta strandi520 – 523Combined sources4
Helixi524 – 535Combined sources12
Beta strandi544 – 546Combined sources3
Helixi558 – 577Combined sources20
Helixi584 – 587Combined sources4
Helixi590 – 598Combined sources9
Helixi604 – 625Combined sources22
Helixi634 – 647Combined sources14
Turni652 – 655Combined sources4
Beta strandi656 – 658Combined sources3
Beta strandi660 – 662Combined sources3
Beta strandi672 – 678Combined sources7
Turni682 – 684Combined sources3
Helixi696 – 699Combined sources4
Helixi708 – 722Combined sources15
Beta strandi723 – 732Combined sources10
Beta strandi736 – 738Combined sources3
Helixi746 – 756Combined sources11
Beta strandi765 – 767Combined sources3
Helixi769 – 780Combined sources12
Helixi791 – 793Combined sources3
Beta strandi794 – 797Combined sources4
Helixi804 – 806Combined sources3
Helixi807 – 810Combined sources4
Helixi834 – 840Combined sources7
Beta strandi841 – 843Combined sources3
Helixi844 – 850Combined sources7
Turni851 – 853Combined sources3
Helixi874 – 889Combined sources16
Helixi894 – 904Combined sources11
Helixi910 – 932Combined sources23
Beta strandi939 – 947Combined sources9
Beta strandi950 – 959Combined sources10
Beta strandi961 – 967Combined sources7
Helixi974 – 989Combined sources16
Beta strandi995 – 999Combined sources5
Helixi1001 – 1003Combined sources3
Beta strandi1005 – 1008Combined sources4
Helixi1013 – 1029Combined sources17
Turni1030 – 1032Combined sources3
Helixi1039 – 1049Combined sources11
Helixi1053 – 1055Combined sources3
Helixi1061 – 1075Combined sources15
Beta strandi1079 – 1081Combined sources3
Helixi1088 – 1091Combined sources4
Helixi1099 – 1117Combined sources19

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[»]
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.
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)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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W36X-ray3.10C/F1-1122[»]
3K70X-ray3.59C/F1-1122[»]
5LD2electron microscopy3.83C1-1122[»]
ProteinModelPortaliP07648.
SMRiP07648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

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.
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: November 30, 2016
This is version 140 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.