Detail Information for IndEnz0002013901
IED ID IndEnz0002013901
Enzyme Type ID protease013901
Protein Name DNA repair protein RadA
EC 3.6.4.-
Branch migration protein RadA
Gene Name radA CT_298
Organism Chlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic Lineage cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia trachomatis Chlamydia trachomatis (strain D/UW-3/Cx)
Enzyme Sequence MTTKIKTQWTCTECGTHSPKWLGQCSGCLQWNTLVEERTAPKLNTSSYSSSSSIPIPLNNVEFQEEIRIHTQAQGWNRLLGGGTVRGSLALLGGEPGIGKSTLLLQISSQFAAAGHKVLYVCGEESVSQTSLRAQRLQISSNNIFLFPETNLEDIKQQIDNIAPDILVIDSIQIIFSPSLSSAPGSVAQVRETTAELMHIAKQKQITTFIIGHVTKSGEIAGPRILEHLVDTVLYFEGNAHANYRMIRSVKNRFGPTNELLILSMHTDGLREVENPSGLFLQEKIVETTGSTIIPIVEGSETLLIEVQALVSSSPFSNPVRKTSGFDPNRFSLLLAVLEKRANVKLYTSDVFLSIAGGLKITQPSADLGAVLSVVSSLYNRYLPKNYTYTGEIGLGGEIRHVSHMEHRIKESIIMGFKGIVMPFGQIKGLPKEFLDQIDIIGVKTIKDAVRLLQ
Enzyme Length 454
Uniprot Accession Number O84300
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 94..101; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01498
Features Chain (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;Reference proteome;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 251..255; /note=RadA KNRFG motif; /evidence=ECO:0000255|HAMAP-Rule:MF_01498
Gene Encoded By
Mass 49,783
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda