Detail Information for IndEnz0002013908
IED ID IndEnz0002013908
Enzyme Type ID protease013908
Protein Name DNA repair protein RadA
EC 3.6.4.-
Branch migration protein RadA
Gene Name radA sms HP_0223
Organism Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Enzyme Sequence MAKKTSLFECQHCGFTSPKWLGKCVQCNAWESFIELNQAQKEVLNTLKKPIPQAQKSVSIAAIEHEEVIKFSSTQSELDIVLGGGIAKGGLYLVGGSPGVGKSTLLLKVASGLAKNQQKVLYVSGEESLSQIKMRAIRLDCIEKELYLLNEINWPVIKANIESENYFACVIDSIQTLYSPEISSAPGSISQVREITFELMRLAKTRDIAIFIIGHITKEGSIAGPRVLEHMVDSVLYFEGDPSRELRILRSFKNRFGPTSEIGLFEMKEQGLVSAKEASSLFFSKEEPMEGSAITITLEGSRALILEIQALVSECSFGSPKRLANGFDTNRLNMLIALLEKKLEIPLNRHDVFINVSGGIKISEPACDLAVIASILSSFKNRKIDNKTAFLGEVSLNGRILEAPNLNARLKEMENYGFLKAILPKKPSQKTSIKCYEANAVGKIVEWM
Enzyme Length 448
Uniprot Accession Number P56148
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 96..103; /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 11196647;
Motif MOTIF 253..257; /note=RadA KNRFG motif; /evidence=ECO:0000255|HAMAP-Rule:MF_01498
Gene Encoded By
Mass 49,451
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda