RADA_ECOLI
ID RADA_ECOLI Reviewed; 460 AA.
AC P24554; Q2M5S8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498, ECO:0000303|PubMed:6754650};
DE EC=3.6.4.- {ECO:0000269|PubMed:26845522};
DE AltName: Full=Branch migration protein RadA {ECO:0000303|PubMed:26845522};
DE AltName: Full=DNA repair protein Sms {ECO:0000303|PubMed:1327967};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498, ECO:0000303|PubMed:6754650};
GN Synonyms=sms {ECO:0000303|PubMed:1327967}; OrderedLocusNames=b4389, JW4352;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, DISRUPTION PHENOTYPE, PUTATIVE
RP ZINC FINGER, AND OPERON.
RC STRAIN=K12;
RX PubMed=1327967; DOI=10.1016/0378-1119(92)90002-7;
RA Neuwald A.F., Berg D.E., Stauffer G.V.;
RT "Mutational analysis of the Escherichia coli serB promoter region reveals
RT transcriptional linkage to a downstream gene.";
RL Gene 120:1-9(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, AND MUTAGENESIS OF CYS-28.
RC STRAIN=K12 / AB1157;
RX PubMed=8759876; DOI=10.1128/jb.178.16.5045-5048.1996;
RA Song Y., Sargentini N.J.;
RT "Escherichia coli DNA repair genes radA and sms are the same gene.";
RL J. Bacteriol. 178:5045-5048(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP ISOLATION OF RADA100 ALLELE, AND MUTAGENESIS OF CYS-28.
RC STRAIN=K12;
RX PubMed=6754650; DOI=10.1080/09553008214551251;
RA Diver W.P., Sargentini N.J., Smith K.C.;
RT "A mutation (radA100) in Escherichia coli that selectively sensitizes cells
RT grown in rich medium to x- or u.v.-radiation, or methyl
RT methanesulphonate.";
RL Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 42:339-346(1982).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-28.
RC STRAIN=K12 / AB1157;
RX PubMed=12446634; DOI=10.1128/jb.184.24.6836-6844.2002;
RA Beam C.E., Saveson C.J., Lovett S.T.;
RT "Role for radA/sms in recombination intermediate processing in Escherichia
RT coli.";
RL J. Bacteriol. 184:6836-6844(2002).
RN [8]
RP FUNCTION.
RC STRAIN=K12 / AB1157;
RX PubMed=16904387; DOI=10.1016/j.dnarep.2006.06.008;
RA Lovett S.T.;
RT "Replication arrest-stimulated recombination: Dependence on the RecA
RT paralog, RadA/Sms and translesion polymerase, DinB.";
RL DNA Repair 5:1421-1427(2006).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25049088; DOI=10.1128/jb.01589-14;
RA Byrne R.T., Chen S.H., Wood E.A., Cabot E.L., Cox M.M.;
RT "Escherichia coli genes and pathways involved in surviving extreme exposure
RT to ionizing radiation.";
RL J. Bacteriol. 196:3534-3545(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25425430; DOI=10.1111/mmi.12885;
RA Chen S.H., Byrne R.T., Wood E.A., Cox M.M.;
RT "Escherichia coli radD (yejH) gene: a novel function involved in radiation
RT resistance and double-strand break repair.";
RL Mol. Microbiol. 95:754-768(2015).
RN [11]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-28; LYS-108;
RP 228-LEU--LEU-460; LYS-258; 275-GLN--LEU-460 AND SER-372.
RC STRAIN=K12 / AB1157;
RX PubMed=25484163; DOI=10.1111/mmi.12899;
RA Cooper D.L., Boyle D.C., Lovett S.T.;
RT "Genetic analysis of Escherichia coli RadA: functional motifs and genetic
RT interactions.";
RL Mol. Microbiol. 95:769-779(2015).
RN [12]
RP FUNCTION, ATPASE ACTIVITY, SSDNA-BINDING, AND MUTAGENESIS OF CYS-28;
RP LYS-108; LYS-258 AND SER-372.
RX PubMed=26845522; DOI=10.7554/elife.10807;
RA Cooper D.L., Lovett S.T.;
RT "Recombinational branch migration by the RadA/Sms paralog of RecA in
RT Escherichia coli.";
RL Elife 5:0-0(2016).
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 (PubMed:26845522). Genetic experiments involving combination of radA
CC mutations with mutations in recA, recB, recG, recJ, recQ, ruvA and ruvC
CC show it plays a role in recombination and recombinational repair,
CC probably involving stabilizing or processing branched DNA or blocked
CC replication forks. Is genetically synergistic to RecG and RuvABC
CC (PubMed:12446634, PubMed:25484163). May be involved in recovery of
CC genetic rearrangements during replication fork breakdown
CC (PubMed:16904387). In combination with RadD is important in recovery
CC from double-strand DNA breaks (DSB) (PubMed:25425430).
CC {ECO:0000269|PubMed:12446634, ECO:0000269|PubMed:16904387,
CC ECO:0000269|PubMed:25425430, ECO:0000269|PubMed:25484163,
CC ECO:0000269|PubMed:26845522}.
CC -!- INDUCTION: Part of the serB-radA operon (PubMed:1327967).
CC {ECO:0000269|PubMed:1327967}.
CC -!- DOMAIN: Has a putative N-terminal zinc-finger, a region with homology
CC to RecA with ATPase motifs including the RadA KNRFG motif
CC (approximately residues 60-290), while the C-terminus is homologous to
CC Lon protease (from about residue 290 to the end, the ribosomal S5
CC domain). In this organism the Lon protease active site Ser-372 is
CC conserved, but not all other bacteria encode Ser at this position
CC (PubMed:1327967, PubMed:8759876). Mutation of Ser-372 has no
CC discernible effect on RadA function, suggesting RadA is not a protease
CC (PubMed:25484163). {ECO:0000255|HAMAP-Rule:MF_01498,
CC ECO:0000269|PubMed:25484163, ECO:0000305|PubMed:1327967,
CC ECO:0000305|PubMed:8759876}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to methyl methanesulfonate,
CC mitomycin C, phleomycin (PubMed:1327967, PubMed:12446634). Has a modest
CC defect in RecA-mediated conjugational DNA recombination; double radA-
CC radD mutants have wild-type levels (PubMed:25425430, PubMed:12446634).
CC 10- to 1000-fold decrease in survival after ionising irradiation (IR)
CC (PubMed:25049088, PubMed:25425430). Double radA-radD deletions have
CC nearly 10(6)-fold lower survival against IR and the double mutant is
CC more severely affected by UV radiation than either of the single
CC mutants alone. The single mutation is more sensitive to dsDNA breaks
CC induced by ciprofloxacin (CFX), the double radA-radD mutant is inviable
CC upon CFX treatment; the SOS response is slightly induced in the single
CC and more induced in the double mutant (PubMed:25425430). Another group
CC showed very slight sensitivity to CFX, UV and azidothymidine (AZT) in
CC single deletion mutants, a radA-recG deletion is extremely sensitive to
CC CFX and AZT, less so to UV. The SOS response is induced in the radA-
CC recG double mutant, indicating spontaneous DNA damage. AZT sensitivity
CC is suppressed by further recA or recF deletions, suggesting AZT-induced
CC DNA gaps are processed into lethal intermediates in a RecA-dependent
CC fashion mediated by RecF. RuvAB suppresses UV, CFX and AZT sensitivity
CC to vaarying degrees. Similarly, radA-uvrD double deletions are also
CC more sensitive to UV, CFX and AZT. Adding a recF mutation almost
CC completely suppresses AZT and partially suppresses UV and CFX
CC sensitivity, suggesting RadA processes a class of intermediates that
CC accumulates in uvrD mutants (PubMed:25484163).
CC {ECO:0000269|PubMed:12446634, ECO:0000269|PubMed:1327967,
CC ECO:0000269|PubMed:25049088, ECO:0000269|PubMed:25425430,
CC ECO:0000269|PubMed:25484163}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
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DR EMBL; X63155; CAA44856.1; -; Genomic_DNA.
DR EMBL; U59449; AAC44380.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97285.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77342.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78378.1; -; Genomic_DNA.
DR PIR; JC1417; JC1417.
DR RefSeq; NP_418806.1; NC_000913.3.
DR RefSeq; WP_001029687.1; NZ_LN832404.1.
DR AlphaFoldDB; P24554; -.
DR SMR; P24554; -.
DR BioGRID; 4262780; 171.
DR BioGRID; 853189; 1.
DR DIP; DIP-10635N; -.
DR IntAct; P24554; 5.
DR STRING; 511145.b4389; -.
DR MEROPS; S16.A04; -.
DR jPOST; P24554; -.
DR PaxDb; P24554; -.
DR PRIDE; P24554; -.
DR EnsemblBacteria; AAC77342; AAC77342; b4389.
DR EnsemblBacteria; BAE78378; BAE78378; BAE78378.
DR GeneID; 948912; -.
DR KEGG; ecj:JW4352; -.
DR KEGG; eco:b4389; -.
DR PATRIC; fig|1411691.4.peg.2296; -.
DR EchoBASE; EB1273; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_6; -.
DR InParanoid; P24554; -.
DR OMA; FELMRLA; -.
DR PhylomeDB; P24554; -.
DR BioCyc; EcoCyc:EG11296-MON; -.
DR BRENDA; 3.6.4.B7; 2026.
DR PRO; PR:P24554; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:EcoCyc.
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:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR GO; GO:0006281; P:DNA repair; IMP:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; IDA:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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 1: Evidence at protein level;
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..460
FT /note="DNA repair protein RadA"
FT /id="PRO_0000187926"
FT ZN_FING 11..28
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498,
FT ECO:0000305|PubMed:1327967"
FT REGION 357..460
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498,
FT ECO:0000305|PubMed:1327967"
FT MOTIF 258..262
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498,
FT ECO:0000305|PubMed:8759876"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498,
FT ECO:0000305|PubMed:1327967"
FT MUTAGEN 28
FT /note="C->Y: In radA100; rich medium-grown cells are
FT sensitive to gamma, X-ray and UV radiation as well as
FT methyl methanesulfonate and hydroxyurea, impaired in repair
FT of dsDNA breaks. Decreased resistance to ciprofloxacin
FT (CFX)."
FT /evidence="ECO:0000269|PubMed:12446634,
FT ECO:0000269|PubMed:25484163, ECO:0000269|PubMed:6754650,
FT ECO:0000269|PubMed:8759876"
FT MUTAGEN 108
FT /note="K->R: Decreased resistance to CFX, semi-dominant to
FT wild-type."
FT /evidence="ECO:0000269|PubMed:25484163"
FT MUTAGEN 228..460
FT /note="Missing: Decreased resistance to CFX."
FT /evidence="ECO:0000269|PubMed:25484163"
FT MUTAGEN 258
FT /note="K->R: Decreased resistance to CFX, semi-dominant to
FT wild-type."
FT /evidence="ECO:0000269|PubMed:25484163"
FT MUTAGEN 275..460
FT /note="Missing: Decreased resistance to CFX."
FT /evidence="ECO:0000269|PubMed:25484163"
FT MUTAGEN 372
FT /note="S->A: Wild-type resistance to CFX; equivalent to the
FT active site Ser of Lon protease."
FT /evidence="ECO:0000269|PubMed:25484163"
SQ SEQUENCE 460 AA; 49472 MW; C03C8BE5367E7BFF CRC64;
MAKAPKRAFV CNECGADYPR WQGQCSACHA WNTITEVRLA ASPMVARNER LSGYAGSAGV
AKVQKLSDIS LEELPRFSTG FKEFDRVLGG GVVPGSAILI GGNPGAGKST LLLQTLCKLA
QQMKTLYVTG EESLQQVAMR AHRLGLPTDN LNMLSETSIE QICLIAEEEQ PKLMVIDSIQ
VMHMADVQSS PGSVAQVRET AAYLTRFAKT RGVAIVMVGH VTKDGSLAGP KVLEHCIDCS
VLLDGDADSR FRTLRSHKNR FGAVNELGVF AMTEQGLREV SNPSAIFLSR GDEVTSGSSV
MVVWEGTRPL LVEIQALVDH SMMANPRRVA VGLEQNRLAI LLAVLHRHGG LQMADQDVFV
NVVGGVKVTE TSADLALLLA MVSSLRDRPL PQDLVVFGEV GLAGEIRPVP SGQERISEAA
KHGFRRAIVP AANVPKKAPE GMQIFGVKKL SDALSVFDDL
