IED ID | IndEnz0002013904 |
Enzyme Type ID | protease013904 |
Protein Name |
DNA repair protein RadA EC 3.6.4.- Branch migration protein RadA DNA repair protein Sms |
Gene Name | radA sms b4389 JW4352 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MAKAPKRAFVCNECGADYPRWQGQCSACHAWNTITEVRLAASPMVARNERLSGYAGSAGVAKVQKLSDISLEELPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAQQMKTLYVTGEESLQQVAMRAHRLGLPTDNLNMLSETSIEQICLIAEEEQPKLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDCSVLLDGDADSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVSNPSAIFLSRGDEVTSGSSVMVVWEGTRPLLVEIQALVDHSMMANPRRVAVGLEQNRLAILLAVLHRHGGLQMADQDVFVNVVGGVKVTETSADLALLLAMVSSLRDRPLPQDLVVFGEVGLAGEIRPVPSGQERISEAAKHGFRRAIVPAANVPKKAPEGMQIFGVKKLSDALSVFDDL |
Enzyme Length | 460 |
Uniprot Accession Number | P24554 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.6.4.- |
Enzyme Function | FUNCTION: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function (PubMed:26845522). Genetic experiments involving combination of radA mutations with mutations in recA, recB, recG, recJ, recQ, ruvA and ruvC show it plays a role in recombination and recombinational repair, probably involving stabilizing or processing branched DNA or blocked replication forks. Is genetically synergistic to RecG and RuvABC (PubMed:12446634, PubMed:25484163). May be involved in recovery of genetic rearrangements during replication fork breakdown (PubMed:16904387). In combination with RadD is important in recovery from double-strand DNA breaks (DSB) (PubMed:25425430). {ECO:0000269|PubMed:12446634, ECO:0000269|PubMed:16904387, ECO:0000269|PubMed:25425430, ECO:0000269|PubMed:25484163, ECO:0000269|PubMed:26845522}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 102..109; /note="ATP"; /evidence="ECO:0000255|HAMAP-Rule:MF_01498, ECO:0000305|PubMed:1327967" |
Features | Chain (1); Motif (1); Mutagenesis (6); Nucleotide binding (1); Region (1); Zinc finger (1) |
Keywords | ATP-binding;DNA damage;DNA repair;DNA-binding;Hydrolase;Metal-binding;Nucleotide-binding;Reference proteome;Stress response;Zinc;Zinc-finger |
Interact With | |
Induction | INDUCTION: Part of the serB-radA operon (PubMed:1327967). {ECO:0000269|PubMed:1327967}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15690043; 16606699; 24561554; |
Motif | MOTIF 258..262; /note="RadA KNRFG motif"; /evidence="ECO:0000255|HAMAP-Rule:MF_01498, ECO:0000305|PubMed:8759876" |
Gene Encoded By | |
Mass | 49,472 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.6.4.B7; |