ID   RADA_STRP1              Reviewed;         453 AA.
AC   Q9A1K1; Q490Z9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 141.
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=SPy_0236, M5005_Spy0200;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(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; AE004092; AAK33316.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ50819.1; -; Genomic_DNA.
DR   RefSeq; NP_268595.1; NC_002737.2.
DR   AlphaFoldDB; Q9A1K1; -.
DR   SMR; Q9A1K1; -.
DR   STRING; 1314.HKU360_00241; -.
DR   MEROPS; S16.A04; -.
DR   PaxDb; Q9A1K1; -.
DR   EnsemblBacteria; AAK33316; AAK33316; SPy_0236.
DR   KEGG; spy:SPy_0236; -.
DR   KEGG; spz:M5005_Spy0200; -.
DR   PATRIC; fig|160490.10.peg.208; -.
DR   HOGENOM; CLU_018264_0_1_9; -.
DR   OMA; FELMRLA; -.
DR   Proteomes; UP000000750; 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..453
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187938"
FT   ZN_FING         10..27
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          350..453
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   MOTIF           251..255
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   453 AA;  49373 MW;  5A04C8589800F54C CRC64;
     MAKKKATFIC QECGYQSPKY LGRCPNCSAW SSFVEEVEVK EVKNARVSLA GEKSRPVKLK
     DVDNISYHRT QTDMSEFNRV LGGGVVPGSL ILIGGDPGIG KSTLLLQVST QLANKGTVLY
     VSGEESAEQI KLRSERLGDI DNEFYLYAET NMQAIRTEIE NIKPDFLIID SIQTIMSPDI
     TGVQGSVSQV REVTAELMQL AKTNNIATFI VGHVTKEGTL AGPRMLEHMV DTVLYFEGER
     HHTFRILRAV KNRFGSTNEI GIFEMQSGGL VEVLNPSQVF LEERLDGATG SAVVVTMEGS
     RPILAEVQSL VTPTVFGNAR RTTTGLDFNR VSLIMAVLEK RCGLLLQNQD AYLKSAGGVK
     LDEPAIDLAV AVAIASSYKE KPTSPQEAFL GEIGLTGEIR RVTRIEQRIN EAAKLGFTKV
     YAPKNALQGI DIPQGIEVVG VTTVGQVLNA VFS