RADA_PSEAE
ID RADA_PSEAE Reviewed; 453 AA.
AC P96963;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=PA4609;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RA Howell M.L., Heur M., Klotz M.G., Hassett D.J.;
RT "Pseudomonas aeruginosa oxidative stress operon.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; U89384; AAB49466.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07997.1; -; Genomic_DNA.
DR PIR; A83069; A83069.
DR RefSeq; NP_253299.1; NC_002516.2.
DR RefSeq; WP_003094867.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P96963; -.
DR SMR; P96963; -.
DR STRING; 287.DR97_1915; -.
DR PaxDb; P96963; -.
DR PRIDE; P96963; -.
DR EnsemblBacteria; AAG07997; AAG07997; PA4609.
DR GeneID; 881107; -.
DR KEGG; pae:PA4609; -.
DR PATRIC; fig|208964.12.peg.4824; -.
DR PseudoCAP; PA4609; -.
DR HOGENOM; CLU_018264_0_1_6; -.
DR InParanoid; P96963; -.
DR OMA; FELMRLA; -.
DR PhylomeDB; P96963; -.
DR BioCyc; PAER208964:G1FZ6-4703-MON; -.
DR Proteomes; UP000002438; 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..453
FT /note="DNA repair protein RadA"
FT /id="PRO_0000187934"
FT ZN_FING 10..27
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 351..453
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 252..256
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT CONFLICT 142
FT /note="E -> K (in Ref. 1; AAB49466)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> D (in Ref. 1; AAB49466)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..244
FT /note="GR -> AA (in Ref. 1; AAB49466)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="L -> M (in Ref. 1; AAB49466)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> F (in Ref. 1; AAB49466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 48411 MW; AAD23FEFAE1EEE05 CRC64;
MAKAKRMYGC TECGATFPKW AGQCADCGAW NTLVETVVEA APSGSGRGGW AGQQANLKTL
AEVSVEEMPR FTTGSTELDR VLGGGLVDGS VVLIGGDPGI GKSTILLQTL CNLASRVPAL
YVTGEESQQQ VAMRARRLSL PEDKLKVMTE TSIETIIATA RQEQPRVMVI DSIQTIFTEQ
LQSAPGGVAQ VRESAAMLVR YAKQSGTAIF LVGHVTKEGA LAGPRVLEHM VDTVLYFEGE
SDGRLRLLRA VKNRFGAVNE LGVFGMTDKG LKEVSNPSAI FLTRAQEAVP GSVVMATWEG
SRPMLVEVQA LVDTSHLANP RRVTLGLDQN RLAMLLAVLH RHGGIPTYDQ DVFLNVVGGV
KVLETASDLA LMAAVMSSLR NRPLPHDLLV FGEVGLSGEV RPVPSGQERL KEAGKHGFKR
AIVPLGNAPK EAPAGLQVIA VTRLEQALDA LFE
