ID   DDRA_DEIRA              Reviewed;         208 AA.
AC   Q9RX92;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Single-stranded DNA-binding protein DdrA;
DE   AltName: Full=DNA damage response protein A;
GN   Name=ddrA; OrderedLocusNames=DR_0423;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-6, FUNCTION, INDUCTION, MASS SPECTROMETRY, DISRUPTION
RP   PHENOTYPE, AND SUBUNIT.
RX   PubMed=15361932; DOI=10.1371/journal.pbio.0020304;
RA   Harris D.R., Tanaka M., Saveliev S.V., Jolivet E., Earl A.M., Cox M.M.,
RA   Battista J.R.;
RT   "Preserving genome integrity: the DdrA protein of Deinococcus radiodurans
RT   R1.";
RL   PLoS Biol. 2:E304-E304(2004).
RN   [3]
RP   INDUCTION, ROLE IN RADIORESISTANCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15454524; DOI=10.1534/genetics.104.029249;
RA   Tanaka M., Earl A.M., Howell H.A., Park M.J., Eisen J.A., Peterson S.N.,
RA   Battista J.R.;
RT   "Analysis of Deinococcus radiodurans's transcriptional response to ionizing
RT   radiation and desiccation reveals novel proteins that contribute to extreme
RT   radioresistance.";
RL   Genetics 168:21-33(2004).
CC   -!- FUNCTION: ssDNA-binding protein that contributes to the ionizing
CC       radiation resistance of D.radiodurans. Plays a role in DNA repair and
CC       genome reconstitution, in a RecA-independent process, since DdrA is
CC       essential for recovery from severe genomic fragmentation as a result of
CC       exposure to severe levels of ionizing radiation in an environment
CC       lacking nutrients. In vitro, binds to the 3'-ends of single-stranded
CC       DNA, protecting them from nuclease degradation. Thus, DdrA is part of a
CC       DNA end-protection system that helps to preserve genome integrity
CC       following irradiation or desiccation. Does not display DNA strand
CC       annealing activity, unlike eukaryotic Rad52 protein homologs.
CC       {ECO:0000269|PubMed:15361932, ECO:0000269|PubMed:15454524}.
CC   -!- SUBUNIT: Homooligomer composed of 8 to 10 subunits; probably arranged
CC       in a ring-structure. {ECO:0000269|PubMed:15361932}.
CC   -!- INDUCTION: Induced to high levels following extreme ionizing radiation
CC       exposure. Also highly induced in response to desiccation stress.
CC       {ECO:0000269|PubMed:15361932, ECO:0000269|PubMed:15454524}.
CC   -!- MASS SPECTROMETRY: Mass=23012.8; Mass_error=3.46; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:15361932};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a normal growth
CC       rate, do not exhibit a decrease in the efficiency of natural
CC       transformation, but display a reduced capacity to survive ionizing
CC       radiation when exposed at doses superior to 2.5 kGy and exhibit
CC       increased sensitivity to mitomycin C. {ECO:0000269|PubMed:15361932,
CC       ECO:0000269|PubMed:15454524}.
CC   -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
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DR   EMBL; AE000513; AAF10011.1; -; Genomic_DNA.
DR   PIR; E75520; E75520.
DR   RefSeq; NP_294146.1; NC_001263.1.
DR   RefSeq; WP_010887068.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RX92; -.
DR   STRING; 243230.DR_0423; -.
DR   EnsemblBacteria; AAF10011; AAF10011; DR_0423.
DR   KEGG; dra:DR_0423; -.
DR   PATRIC; fig|243230.17.peg.597; -.
DR   eggNOG; COG4712; Bacteria.
DR   HOGENOM; CLU_113751_0_0_0; -.
DR   OMA; CAVQFGI; -.
DR   OrthoDB; 1614956at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0071465; P:cellular response to desiccation; IEP:UniProtKB.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IEP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR   InterPro; IPR041247; Rad52_fam.
DR   Pfam; PF04098; Rad52_Rad22; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA damage; DNA repair; DNA-binding;
KW   Reference proteome; Stress response.
FT   CHAIN           1..208
FT                   /note="Single-stranded DNA-binding protein DdrA"
FT                   /id="PRO_0000394495"
SQ   SEQUENCE   208 AA;  23002 MW;  D91A2C42DA086A53 CRC64;
     MKLSDVQKRL QAPFPAHTVS WKPAAFNAER TRALLLAHVD ARAVQDRLDA VCPDDWSFEM
     EVVSGAEVPT VKGRLTVLGV TREDIGEAPE GSMAAYKAAA SDAMKRCAVQ FGIGRYLYDL
     PKQWADWDDA RRGPKHLPEL PEWARPDHER TPGGAHLVQA MEQLRYELPE DLDLQREVYK
     HLKAALGSIH PVPTGPVPTN PVQGGRAA