| IED ID | IndEnz0002001323 |
| Enzyme Type ID | protease001323 |
| Protein Name |
RecBCD enzyme subunit RecC EC 3.1.11.5 Exodeoxyribonuclease V 125 kDa polypeptide Exodeoxyribonuclease V gamma chain Exonuclease V subunit RecC ExoV subunit RecC |
| Gene Name | recC b2822 JW2790 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MLRVYHSNRLDVLEALMEFIVERERLDDPFEPEMILVQSTGMAQWLQMTLSQKFGIAANIDFPLPASFIWDMFVRVLPEIPKESAFNKQSMSWKLMTLLPQLLEREDFTLLRHYLTDDSDKRKLFQLSSKAADLFDQYLVYRPDWLAQWETGHLVEGLGEAQAWQAPLWKALVEYTHQLGQPRWHRANLYQRFIETLESATTCPPGLPSRVFICGISALPPVYLQALQALGKHIEIHLLFTNPCRYYWGDIKDPAYLAKLLTRQRRHSFEDRELPLFRDSENAGQLFNSDGEQDVGNPLLASWGKLGRDYIYLLSDLESSQELDAFVDVTPDNLLHNIQSDILELENRAVAGVNIEEFSRSDNKRPLDPLDSSITFHVCHSPQREVEVLHDRLLAMLEEDPTLTPRDIIVMVADIDSYSPFIQAVFGSAPADRYLPYAISDRRARQSHPVLEAFISLLSLPDSRFVSEDVLALLDVPVLAARFDITEEGLRYLRQWVNESGIRWGIDDDNVRELELPATGQHTWRFGLTRMLLGYAMESAQGEWQSVLPYDESSGLIAELVGHLASLLMQLNIWRRGLAQERPLEEWLPVCRDMLNAFFLPDAETEAAMTLIEQQWQAIIAEGLGAQYGDAVPLSLLRDELAQRLDQERISQRFLAGPVNICTLMPMRSIPFKVVCLLGMNDGVYPRQLAPLGFDLMSQKPKRGDRSRRDDDRYLFLEALISAQQKLYISYIGRSIQDNSERFPSVLVQELIDYIGQSHYLPGDEALNCDESEARVKAHLTCLHTRMPFDPQNYQPGERQSYAREWLPAASQAGKAHSEFVQPLPFTLPETVPLETLQRFWAHPVRAFFQMRLQVNFRTEDSEIPDTEPFILEGLSRYQINQQLLNALVEQDDAERLFRRFRAAGDLPYGAFGEIFWETQCQEMQQLADRVIACRQPGQSMEIDLACNGVQITGWLPQVQPDGLLRWRPSLLSVAQGMQLWLEHLVYCASGGNGESRLFLRKDGEWRFPPLAAEQALHYLSQLIEGYREGMSAPLLVLPESGGAWLKTCYDAQNDAMLDDDSTLQKARTKFLQAYEGNMMVRGEGDDIWYQRLWRQLTPETMEAIVEQSQRFLLPLFRFNQS |
| Enzyme Length | 1122 |
| Uniprot Accession Number | P07648 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: 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 Mg(2+) (13 mM MgCl(2+)) or incubation with DNase allow holoenyzme reassembly, suggesting it is DNA bound to RecB that prevents reassembly (PubMed:10197988). {ECO:0000269|PubMed:10197988, ECO:0000269|PubMed:1535156}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01486}; |
| DNA Binding | DNA_BIND 971; DNA_BIND 1001; DNA_BIND 1078..1081 |
| EC Number | 3.1.11.5 |
| Enzyme Function | FUNCTION: 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. {ECO:0000269|PubMed:10197988, ECO:0000269|PubMed:10884344, ECO:0000269|PubMed:123277, ECO:0000269|PubMed:12815437, ECO:0000269|PubMed:12815438, ECO:0000269|PubMed:1535156, ECO:0000269|PubMed:16041061, ECO:0000269|PubMed:1618858, ECO:0000269|PubMed:20852646, ECO:0000269|PubMed:23851395, ECO:0000269|PubMed:4268693, ECO:0000269|PubMed:4552016, ECO:0000269|PubMed:4562392, ECO:0000269|PubMed:7608206, ECO:0000269|PubMed:9192629, ECO:0000269|PubMed:9230304, ECO:0000269|PubMed:9448271, ECO:0000269|PubMed:9790841}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (29); Chain (1); DNA binding (3); Helix (52); Mutagenesis (10); Natural variant (1); Turn (7) |
| Keywords | 3D-structure;ATP-binding;DNA damage;DNA repair;DNA-binding;Direct protein sequencing;Exonuclease;Helicase;Hydrolase;Nuclease;Nucleotide-binding;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (13); X-ray crystallography (2) |
| Cross Reference PDB | 1W36; 3K70; 5LD2; 5MBV; 6SJB; 6SJE; 6SJF; 6SJG; 6T2U; 6T2V; 7MR0; 7MR1; 7MR2; 7MR3; 7MR4; |
| Mapped Pubmed ID | 15690043; 16606699; 27644322; 28009252; 31907455; 34246654; |
| Motif | |
| Gene Encoded By | |
| Mass | 128,848 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.1.11.5; |