ID   RADA_HAEIN              Reviewed;         458 AA.
AC   P45266;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, 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=HI_1597;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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=AAC23242.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC23242.1; ALT_INIT; Genomic_DNA.
DR   PIR; I64131; I64131.
DR   RefSeq; NP_439739.2; NC_000907.1.
DR   RefSeq; WP_005693612.1; NC_000907.1.
DR   AlphaFoldDB; P45266; -.
DR   SMR; P45266; -.
DR   STRING; 71421.HI_1597; -.
DR   MEROPS; S16.004; -.
DR   DNASU; 950453; -.
DR   EnsemblBacteria; AAC23242; AAC23242; HI_1597.
DR   KEGG; hin:HI_1597; -.
DR   PATRIC; fig|71421.8.peg.1670; -.
DR   eggNOG; COG1066; Bacteria.
DR   HOGENOM; CLU_018264_0_1_6; -.
DR   PhylomeDB; P45266; -.
DR   BioCyc; HINF71421:G1GJ1-1610-MON; -.
DR   Proteomes; UP000000579; 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..458
FT                   /note="DNA repair protein RadA"
FT                   /id="PRO_0000187927"
FT   ZN_FING         11..28
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   REGION          355..458
FT                   /note="Lon-protease-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   MOTIF           256..260
FT                   /note="RadA KNRFG motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ   SEQUENCE   458 AA;  49371 MW;  5AA547FCD17630B2 CRC64;
     MAKAPKTAYV CNDCGAEFSR WQGQCSACKA WNTITEVRLI STAKSKNDRF SGYAGETQAK
     IQTLSEISLQ ETPRFSSGFS ELDRVLGGGI VPGSAILIGG HPGAGKSTLL LQVMCGLAKN
     MTALYVTGEE SLQQVAMRAS RLGLPSDQLK MLSETSVEQI CNLADQLKPQ IIVVDSIQVM
     HLADIQSSPG SVAQVRECAS FLTRYAKTRQ VAIIMVGHVT KDGTLAGPKV LEHAIDCSLL
     LEGEADSRYR TLRSHKNRFG AVNELGVFGM TEQGLREVKN PSAIFLSRGD EITSGSSVMV
     LWEGTRPLLV EIQALVDHSM LANPRRVAVG LEQNRLALLL AVLHRHGGLQ MADQDVFVNV
     VGGVKVSETS ADLALLLALI SSFRNRPLPQ DLVIFGEVGL AGEIRPVPSG QERISEAAKH
     GFKRAIVPFG NKPKSAVENM QVFTVKKLTD ALAVLDNL