ID   RADA_SYNY3              Reviewed;         505 AA.
AC   P74391;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 139.
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}; Synonyms=sms;
GN   OrderedLocusNames=slr0448;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18488.1; -; Genomic_DNA.
DR   PIR; S76229; S76229.
DR   AlphaFoldDB; P74391; -.
DR   SMR; P74391; -.
DR   STRING; 1148.1653575; -.
DR   MEROPS; S16.A04; -.
DR   PaxDb; P74391; -.
DR   EnsemblBacteria; BAA18488; BAA18488; BAA18488.
DR   KEGG; syn:slr0448; -.
DR   eggNOG; COG1066; Bacteria.
DR   InParanoid; P74391; -.
DR   OMA; FELMRLA; -.
DR   PhylomeDB; P74391; -.
DR   Proteomes; UP000001425; 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; IBA:GO_Central.
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; 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..505
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187942"
FT   ZN_FING         10..27
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          380..505
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          485..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           281..285
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   BINDING         107..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   505 AA;  54191 MW;  EC2F52A3B5254609 CRC64;
     MAKARTKFVC SACGADHAQW FGRCPKCHEY GSLQEEIVNA VSSGTNHRSL GAQKSRSSKV
     KTGQPQAALT FSQIRQENQG RFLSGYGELD RVLGGGIVPG ALILIGGDPG IGKSTLLLQV
     AFQLATRLPR ILYVSAEESG QQIKLRATRL GITQTVEPSQ AQDGINNLAH DGNLFVLPET
     NLDDILRELE ALQPQVAIID SIQNLYFPAL SSAPGSVSQV RECTGLLMQL AKRDHISLFI
     VGHVTKEGAI AGPKVLEHLV DTVLYFQGDR FASHRLLRSV KNRFGATQEI GIFEMVQSGL
     QEVLNPSQLF LGSREEFMSG TAITVACEGT RPLVVELQAL VSPTSYASPR RSTTGVDYNR
     LLQVLAVLEK RLGVPLSKLD AYLSVAGGLE VEEPAVDLAM AIALVASFRD RVVDPTMIIL
     GEIGLGGQIR PVSQLEIRLK EAAKLGFKKA IVPKGQTGIE SAGIKLIPVG KVFAAIAVAL
     PANENTTDQG NGSEAKIEED LGKKD