RADA_RICFE
ID RADA_RICFE Reviewed; 446 AA.
AC Q4UL56;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=RF_0866;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61717.1; -; Genomic_DNA.
DR RefSeq; WP_011271194.1; NC_007109.1.
DR AlphaFoldDB; Q4UL56; -.
DR SMR; Q4UL56; -.
DR STRING; 315456.RF_0866; -.
DR MEROPS; S16.A04; -.
DR EnsemblBacteria; AAY61717; AAY61717; RF_0866.
DR KEGG; rfe:RF_0866; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_5; -.
DR OMA; FELMRLA; -.
DR OrthoDB; 505485at2; -.
DR Proteomes; UP000008548; 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..446
FT /note="DNA repair protein RadA"
FT /id="PRO_0000286660"
FT ZN_FING 10..27
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 349..446
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 250..254
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ SEQUENCE 446 AA; 48329 MW; 344951779B8D9FEB CRC64;
MTKDKKHYIC SNCGNTSPKW SGQCFDCGVW GSIVEEIVST NKAIVKTGSK QDFDKLSGHV
AEQLRIPTPI GELNRVLGGG LVLGSAILIG GDPGIGKSTL LLQLAASNFA SKMNCLYITG
EESLDQIKLR AIRLNLTNYN TDILAATNLE DIIASIEANK NNIDLVVIDS IQTITTKELS
SPPGTVSQIR ICANELVNYA KQNNIIILLS CHVTKDGQLA GPKILEHLVD TVLYFEGDHN
NHFRILRSYK NRFGGVGEIG VFEMCGSGLI EVTNPSELFL MKREQNVIGT SIFAGIEGSR
PLLMEVQALI VPSNMVTPRR SAVGWDANRL SMILAVLSSR IGLNLANYEV YLSIAGGLKI
ADPASDLAVA ASLISAATGK PVPEHSVFFG EISLSGEIRK TAKAETRIKE AVKLGFNKII
CSKLENLTYD FISSVSHLKD LKEIIR