ID   RADA_BRUA2              Reviewed;         467 AA.
AC   Q2YMH5;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01498};
DE   AltName: Full=Branch migration protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
GN   Name=radA {ECO:0000255|HAMAP-Rule:MF_01498}; OrderedLocusNames=BAB1_0474;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=2308;
RX   PubMed=16816190; DOI=10.1128/jb.01994-05;
RA   Roux C.M., Booth N.J., Bellaire B.H., Gee J.M., Roop R.M. II, Kovach M.E.,
RA   Tsolis R.M., Elzer P.H., Ennis D.G.;
RT   "RecA and RadA proteins of Brucella abortus do not perform overlapping
RT   protective DNA repair functions following oxidative burst.";
RL   J. Bacteriol. 188:5187-5195(2006).
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:0000255|HAMAP-Rule:MF_01498}.
CC   -!- DOMAIN: Has a putative N-terminal zinc-finger, a middle region with
CC       homology to RecA with ATPase motifs including the RadA KNRFG motif,
CC       while the C-terminus is homologous to Lon protease. {ECO:0000255|HAMAP-
CC       Rule:MF_01498}.
CC   -!- DISRUPTION PHENOTYPE: No alteration in UV resistance; does not replace
CC       RecA. {ECO:0000269|PubMed:16816190}.
CC   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01498}.
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; AM040264; CAJ10430.1; -; Genomic_DNA.
DR   RefSeq; WP_002963605.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YMH5; -.
DR   SMR; Q2YMH5; -.
DR   STRING; 359391.BAB1_0474; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; CAJ10430; CAJ10430; BAB1_0474.
DR   GeneID; 3788891; -.
DR   KEGG; bmf:BAB1_0474; -.
DR   PATRIC; fig|359391.11.peg.2514; -.
DR   HOGENOM; CLU_018264_0_1_5; -.
DR   OMA; FELMRLA; -.
DR   PhylomeDB; Q2YMH5; -.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01498; RadA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004504; DNA_repair_RadA.
DR   InterPro; IPR014774; KaiC-like_dom.
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; PF06745; ATPase; 1.
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; DNA damage; DNA repair; DNA-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..467
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000435880"
FT   ZN_FING         10..27
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          359..467
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   MOTIF           260..264
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   BINDING         98..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   467 AA;  49024 MW;  30EBC8ABAA4F0239 CRC64;
     MAKTRVQFIC QNCGAVHSRW AGKCDSCGEW NTLIEEGTNS GIGSGPAAML SKRKGRAVAL
     TSLSGEIEDA PRIVSGISEL DRVTGGGFVR GSALLIGGDP GIGKSTLLTQ AAAALSNRGH
     RIVYVSGEEA VAQIRLRAQR LGVAASAVEL AAETNVEDII ATISSDNSGS KRPDLVIIDS
     IQTLWTDMAD SAPGTVTQVR SSAQAMIRYA KQTGAAVVLV GHVTKDGQIA GPRVVEHMVD
     GVLYFEGEGG HHYRILRTVK NRFGPTDEIG VFEMSDGGLR EVSNPSELFL GERNEKSPGA
     AVFAGMEGTR PVLVEIQALV APSSLGTPRR AVVGWDGGRL AMILAVLESH CGVRFGQHDV
     YLNVAGGYRI SEPAADIAVA AALVSSMAGI ALPPDCVYFG EISLSGAVRA VSHAVQRLKE
     AEKLGFRQAE VPNGSGELWK DRNFRLMETA ALADLVARIA ASGAGKK