ID   RADA_RICCN              Reviewed;         444 AA.
AC   Q92HG1;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=RC0810;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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   -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01498}.
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DR   EMBL; AE006914; AAL03348.1; -; Genomic_DNA.
DR   PIR; B97801; B97801.
DR   RefSeq; WP_010977421.1; NC_003103.1.
DR   AlphaFoldDB; Q92HG1; -.
DR   SMR; Q92HG1; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; AAL03348; AAL03348; RC0810.
DR   KEGG; rco:RC0810; -.
DR   PATRIC; fig|272944.4.peg.920; -.
DR   HOGENOM; CLU_018264_0_1_5; -.
DR   OMA; FELMRLA; -.
DR   Proteomes; UP000000816; Chromosome.
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   CDD; cd01121; Sms; 1.
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; 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; DNA damage; DNA repair; DNA-binding; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..444
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187935"
FT   ZN_FING         8..25
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          347..444
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   MOTIF           248..252
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   444 AA;  48227 MW;  F8BE0DFB5E5C63FE CRC64;
     MTKKHYICSN CGNISPKWSG QCFDCGVWGS IVEEIISTNQ VIVKVGSKQD FDKLSGHVTE
     QLRIPTPIGE FNRVLGGGLV LGSAILIGGD PGIGKSTLLL QLAASNFASK MNCLYITGEE
     SLDQIKLRAI RLNLTNYNTD ILAATNLENI IASIEANKNN IDLIVIDSIQ TITTKELSSP
     PGTVSQIRTC ANELVNYAKQ NNIIILLSCH VTKDGQLAGP KILEHLVDTV LYFEGDHNNH
     FRILRSYKNR FGGVGEIGVF EMSGSGLIEV TNPSELFLMQ REQNVIGTSI FAGIEGSRPL
     LMEVQALMVP SNMVTPRRSA VGWDANRLSM ILAVLSSRIG LNLANYEVYL SIAGGLKIAD
     PASDLAVTAS LISAATGNPV PEHSVFFGEI SLSGEIRKTA KAETRIKEAV KLGFNKIICS
     KFENLTYDFI SSVSHLKDLK EIIK