ID A0A2J9HBQ6_BURGL Unreviewed; 458 AA. AC A0A2J9HBQ6; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 12-AUG-2020, entry version 11. DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}; GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498}; GN ORFNames=CEQ24_023435 {ECO:0000313|EMBL:PNL01906.1}; OS Burkholderia glumae (Pseudomonas glumae). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=337 {ECO:0000313|EMBL:PNL01906.1, ECO:0000313|Proteomes:UP000197337}; RN [1] {ECO:0000313|Proteomes:UP000197337} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_346 {ECO:0000313|Proteomes:UP000197337}; RA Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L., RA Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K., RA Aluvathingal J., Nadendla S., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent ATPase involved in processing of recombination CC intermediates, plays a role in repairing DNA breaks. Stimulates the CC branch migration of RecA-mediated strand transfer reactions, allowing CC the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA CC in the presence of ADP but not other nucleotides, has ATPase activity CC that is stimulated by ssDNA and various branched DNA structures, but CC inhibited by SSB. Does not have RecA's homology-searching function. CC {ECO:0000256|RuleBase:RU003555}. CC -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably CC involving stabilizing or processing branched DNA or blocked replication CC forks. {ECO:0000256|HAMAP-Rule:MF_01498}. CC -!- DOMAIN: The middle region has homology to RecA with ATPase motifs CC including the RadA KNRFG motif, while the C-terminus is homologous to CC Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}. CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PNL01906.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NJFN02000003; PNL01906.1; -; Genomic_DNA. DR RefSeq; WP_015875305.1; NZ_QTQU01000001.1. DR GeneID; 45697666; -. DR Proteomes; UP000197337; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule. DR CDD; cd01121; Sms; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_01498; RadA_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004504; DNA_repair_RadA. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR041166; Rubredoxin_2. DR Pfam; PF18073; Rubredoxin_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00416; sms; 1. DR PROSITE; PS50162; RECA_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01498, ECO:0000256|RuleBase:RU003555}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498, KW ECO:0000256|RuleBase:RU003555}; KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP- KW Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}. FT DOMAIN 65..218 FT /note="RECA_2" FT /evidence="ECO:0000259|PROSITE:PS50162" FT NP_BIND 94..101 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498" FT REGION 354..458 FT /note="Lon-protease-like" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498" FT MOTIF 255..259 FT /note="RadA KNRFG motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498" SQ SEQUENCE 458 AA; 48595 MW; 0DEAB1C624D4840B CRC64; MAKQKTVYVC TACGGQSPKW QGQCPACHAW NTLLESAAET PSSHRFQALA KSAPVQRLAD IDAADVPRFT TGIGEFDRVL GGGLVAGGVV LIGGDPGIGK STLLLQSLAQ LASQRRALYI SGEESAAQIA LRAQRLALLD HGGDAADLKL LAEIQLEKIQ ATIDAERPDV AVIDSIQTVY SDALSSAPGS VAQVRECAAQ LTRIAKQSGT AIIMVGHVTK EGALAGPRVL EHIVDTVLYF EGDTHSSYRL VRAIKNRFGA VNELGVFAMT ERGLRGVANP SALFLSQHEE VVPGSCVLVT QEGSRPLLVE VQALVDTANV PNPRRLAVGL EQNRLAMLLA VLHRHAGIAC FDQDVFLNAV GGVKITEPAA DLAVLLAIHS SMRNKALPKG LIVFGEVGLA GEIRPSPRGQ ERLREAAKLG FTMALIPKAN APKQPIEGLT VMAVERIEQA IDRVRGLE //