ID   RADA_CHLTR              Reviewed;         454 AA.
AC   O84300;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
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=CT_298;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(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}.
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DR   EMBL; AE001273; AAC67891.1; -; Genomic_DNA.
DR   PIR; D71532; D71532.
DR   RefSeq; NP_219803.1; NC_000117.1.
DR   RefSeq; WP_009871646.1; NC_000117.1.
DR   AlphaFoldDB; O84300; -.
DR   SMR; O84300; -.
DR   STRING; 813.O172_01605; -.
DR   EnsemblBacteria; AAC67891; AAC67891; CT_298.
DR   GeneID; 884816; -.
DR   KEGG; ctr:CT_298; -.
DR   PATRIC; fig|272561.5.peg.320; -.
DR   HOGENOM; CLU_018264_0_1_0; -.
DR   InParanoid; O84300; -.
DR   OMA; FELMRLA; -.
DR   Proteomes; UP000000431; 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; 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..454
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187925"
FT   ZN_FING         11..28
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          350..454
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         94..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   454 AA;  49783 MW;  CD5DD671BC2A9E27 CRC64;
     MTTKIKTQWT CTECGTHSPK WLGQCSGCLQ WNTLVEERTA PKLNTSSYSS SSSIPIPLNN
     VEFQEEIRIH TQAQGWNRLL GGGTVRGSLA LLGGEPGIGK STLLLQISSQ FAAAGHKVLY
     VCGEESVSQT SLRAQRLQIS SNNIFLFPET NLEDIKQQID NIAPDILVID SIQIIFSPSL
     SSAPGSVAQV RETTAELMHI AKQKQITTFI IGHVTKSGEI AGPRILEHLV DTVLYFEGNA
     HANYRMIRSV KNRFGPTNEL LILSMHTDGL REVENPSGLF LQEKIVETTG STIIPIVEGS
     ETLLIEVQAL VSSSPFSNPV RKTSGFDPNR FSLLLAVLEK RANVKLYTSD VFLSIAGGLK
     ITQPSADLGA VLSVVSSLYN RYLPKNYTYT GEIGLGGEIR HVSHMEHRIK ESIIMGFKGI
     VMPFGQIKGL PKEFLDQIDI IGVKTIKDAV RLLQ