Detail Information for IndEnz0002013931
IED ID IndEnz0002013931
Enzyme Type ID protease013931
Protein Name DNA repair protein RadA
EC 3.6.4.-
Branch migration protein RadA
Gene Name radA sms TP_1022
Organism Treponema pallidum (strain Nichols)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Spirochaetales Treponemataceae Treponema Treponema pallidum Treponema pallidum subsp. pallidum (syphilis treponeme) Treponema pallidum (strain Nichols)
Enzyme Sequence MAKKTERAFSCVGCGYVHPKWLGRCPECGEWNSFEETPSLSSGDVRAVKKASSSPVQAFPLCAVRAQDAQRISCGIAEFDRVLGGGAVRRSAIMIGGEPGIGKSTLLLQIAAACGKSVLYVSGEESPGQIRGRADRLNIPIQNIELLCATRVEDVERVLNTRCPTFVIVDSIQTVFSPEAGAIPMTINQLKYCANELIAWVKERDSVLFFTAHVTKDGNIAGPKVVEHMVDTVISFERNEEDIRFLRALKNRFGSVDELGIFTMGENGLSAVQDTAGFFISTRQGMFPVGSATVPVCEGSRVFMVEIQALTVPAKSSVTRVFSDRIDSARVSRVAAVIEKRVGLKFSDQDIYVNVAGGIRLYEPAVDVALAMALYSARQNTPVKTNAAFIGEVSLSGEIRPVRRLKTRLKTAYGLGFSTIYVPIGVEHDTPPPYTLRVVGTLAQTIAEIFSKAKA
Enzyme Length 455
Uniprot Accession Number O83985
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 97..104; /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 250..254; /note=RadA KNRFG motif; /evidence=ECO:0000255|HAMAP-Rule:MF_01498
Gene Encoded By
Mass 49,305
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda