Detail Information for IndEnz0002013904
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;