ID   RADA_RICPR              Reviewed;         445 AA.
AC   Q9ZD04;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=RP546;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA14995.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ235272; CAA14995.1; ALT_INIT; Genomic_DNA.
DR   PIR; A71659; A71659.
DR   RefSeq; NP_220919.1; NC_000963.1.
DR   RefSeq; WP_004597838.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZD04; -.
DR   SMR; Q9ZD04; -.
DR   STRING; 272947.RP546; -.
DR   MEROPS; S16.A04; -.
DR   EnsemblBacteria; CAA14995; CAA14995; CAA14995.
DR   KEGG; rpr:RP546; -.
DR   PATRIC; fig|272947.5.peg.557; -.
DR   eggNOG; COG1066; Bacteria.
DR   HOGENOM; CLU_018264_0_1_5; -.
DR   Proteomes; UP000002480; 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; Reference proteome; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..445
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187936"
FT   ZN_FING         10..27
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          348..445
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   MOTIF           249..253
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   445 AA;  48719 MW;  4CB05571D3122F7D CRC64;
     MTRDKKYYIC SNCANISNKW SGQCFDCGVW GSIVEEIINT NKSIIKGSKQ TFDKLSCNVS
     EQLRIPTPIC ELNRVLGGGL VLGSAILIGG EPGIGKSTLL LQLTASNFES EMRCLYITGE
     ESLDQIKLRA IRLNITNYNT AILAATNLED IIASIDDNNN NIDLVVIDSI QTITTKELSS
     PPGTVSQIRT CANELVNYSK QNNIIILLSC HVTKDGQIAG PKILEHLVDT VLYFEGDHNN
     HFRILRSYKN RFGGVGEIGV FEMSNSGIIE VTNHSELFLI KREHNVVGTS IFAGIEGSRP
     LLMEVQALIV PSNMVTPRRS AVGWDANRLS MILAVLSSRI GLNLANYEIY LSIAGGLKIA
     DPASDLAVAA SLISAATSIP LPEHSVFFGE ISLSGEIRKT AKAETRIKEA VKLGFNKVIC
     SKLENLTYDF IFPCAHLQEL KEIIK