Detail Information for IndEnz0002013899
IED ID IndEnz0002013899
Enzyme Type ID protease013899
Protein Name DNA repair protein RadA
EC 3.6.4.-
Branch migration protein RadA
Gene Name radA TC_0571
Organism Chlamydia muridarum (strain MoPn / Nigg)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia muridarum Chlamydia muridarum (strain MoPn / Nigg)
Enzyme Sequence MTTTKIKTQWACSECGSYSPKWLGQCPGCFQWNTLVEEIHSSKLKTSSYPLSSTTPVPLNTVKFQEEIRISTRSKGWNRLLGGGTVCGSLTLLGGEPGIGKSTLLLQISSQFAEQGYKVLYVCGEESVSQTSLRAQRLQISSSNIFLFPETNLEDIKQQISDLAPDILIIDSIQIIFSPSLSSAPGSVAQVRETTAELMHIAKQKQITTFIIGHVTKSGEIAGPRILEHLVDTVLYFEGNAHTNYRMIRSVKNRFGPTNELLILSMQTDGLHEVENPSGFFLQEKVVETTGSTIIPIVEGSETLLVEVQALVSSSPFSNPVRKTSGFDPNRFSLLLAVLEKRANVKLYTSDVFLSIAGGLKITQPSADLGAVLSVVSSLYNRYLPKNYTYTGEIGLGGEIRHVTHIEHRIKESIIMGFKGIVMPSGQIKGLPKEYLDQIDIIGVKTIKDAVRLLQ
Enzyme Length 455
Uniprot Accession Number Q9PK96
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. {ECO:0000255|HAMAP-Rule:MF_01498}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 95..102; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01498
Features Chain (1); Erroneous initiation (1); Motif (1); Nucleotide binding (1); Region (1); Zinc finger (1)
Keywords ATP-binding;DNA damage;DNA repair;DNA-binding;Hydrolase;Metal-binding;Nucleotide-binding;Stress response;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 252..256; /note=RadA KNRFG motif; /evidence=ECO:0000255|HAMAP-Rule:MF_01498
Gene Encoded By
Mass 49,951
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda