| IED ID | IndEnz0002001322 |
| Enzyme Type ID | protease001322 |
| Protein Name |
RecBCD enzyme subunit RecB EC 3.1.11.5 Exodeoxyribonuclease V 135 kDa polypeptide Exodeoxyribonuclease V beta chain Exonuclease V subunit RecB ExoV subunit RecB Helicase/nuclease RecBCD subunit RecB |
| Gene Name | recB ior rorA b2820 JW2788 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSDVAETLDPLRLPLQGERLIEASAGTGKTFTIAALYLRLLLGLGGSAAFPRPLTVEELLVVTFTEAATAELRGRIRSNIHELRIACLRETTDNPLYERLLEEIDDKAQAAQWLLLAERQMDEAAVFTIHGFCQRMLNLNAFESGMLFEQQLIEDESLLRYQACADFWRRHCYPLPREIAQVVFETWKGPQALLRDINRYLQGEAPVIKAPPPDDETLASRHAQIVARIDTVKQQWRDAVGELDALIESSGIDRRKFNRSNQAKWIDKISAWAEEETNSYQLPESLEKFSQRFLEDRTKAGGETPRHPLFEAIDQLLAEPLSIRDLVITRALAEIRETVAREKRRRGELGFDDMLSRLDSALRSESGEVLAAAIRTRFPVAMIDEFQDTDPQQYRIFRRIWHHQPETALLLIGDPKQAIYAFRGADIFTYMKARSEVHAHYTLDTNWRSAPGMVNSVNKLFSQTDDAFMFREIPFIPVKSAGKNQALRFVFKGETQPAMKMWLMEGESCGVGDYQSTMAQVCAAQIRDWLQAGQRGEALLMNGDDARPVRASDISVLVRSRQEAAQVRDALTLLEIPSVYLSNRDSVFETLEAQEMLWLLQAVMTPERENTLRSALATSMMGLNALDIETLNNDEHAWDVVVEEFDGYRQIWRKRGVMPMLRALMSARNIAENLLATAGGERRLTDILHISELLQEAGTQLESEHALVRWLSQHILEPDSNASSQQMRLESDKHLVQIVTIHKSKGLEYPLVWLPFITNFRVQEQAFYHDRHSFEAVLDLNAAPESVDLAEAERLAEDLRLLYVALTRSVWHCSLGVAPLVRRRGDKKGDTDVHQSALGRLLQKGEPQDAAGLRTCIEALCDDDIAWQTAQTGDNQPWQVNDVSTAELNAKTLQRLPGDNWRVTSYSGLQQRGHGIAQDLMPRLDVDAAGVASVVEEPTLTPHQFPRGASPGTFLHSLFEDLDFTQPVDPNWVREKLELGGFESQWEPVLTEWITAVLQAPLNETGVSLSQLSARNKQVEMEFYLPISEPLIASQLDTLIRQFDPLSAGCPPLEFMQVRGMLKGFIDLVFRHEGRYYLLDYKSNWLGEDSSAYTQQAMAAAMQAHRYDLQYQLYTLALHRYLRHRIADYDYEHHFGGVIYLFLRGVDKEHPQQGIYTTRPNAGLIALMDEMFAGMTLEEA |
| Enzyme Length | 1180 |
| Uniprot Accession Number | P08394 |
| Absorption | |
| Active Site | ACT_SITE 1080; /note="For nuclease activity"; /evidence="ECO:0000269|PubMed:10518611, ECO:0000269|PubMed:9790841" |
| 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_01485}; |
| DNA Binding | DNA_BIND 252..254; DNA_BIND 511..512; DNA_BIND 560..561; DNA_BIND 761 |
| 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 contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. 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:10518611, ECO:0000269|PubMed:10766864, 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:16388588, ECO:0000269|PubMed:18079176, ECO:0000269|PubMed:20852646, ECO:0000269|PubMed:23851395, ECO:0000269|PubMed:25073102, 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 | NP_BIND 23..30; /note=ATP |
| Features | Active site (1); Beta strand (34); Chain (1); DNA binding (4); Domain (2); Helix (57); Initiator methionine (1); Metal binding (4); Mutagenesis (6); Nucleotide binding (1); Region (2); Turn (7) |
| Keywords | 3D-structure;ATP-binding;DNA damage;DNA repair;DNA-binding;Direct protein sequencing;Exonuclease;Helicase;Hydrolase;Magnesium;Metal-binding;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 | 133,959 |
| Kinetics | |
| Metal Binding | METAL 956; /note=Magnesium; via tele nitrogen; /evidence=ECO:0000305; METAL 1067; /note=Magnesium; /evidence=ECO:0000305; METAL 1080; /note=Magnesium; /evidence=ECO:0000305; METAL 1081; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000305 |
| Rhea ID | |
| Cross Reference Brenda | 3.1.11.5; |