ID   DDRA_DEIDV              Reviewed;         201 AA.
AC   C1D1R8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Single-stranded DNA-binding protein DdrA;
DE   AltName: Full=DNA damage response protein A;
GN   Name=ddrA; OrderedLocusNames=Deide_09150;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
RN   [2]
RP   FUNCTION AS A DNA-BINDING PROTEIN, ROLE IN RADIORESISTANCE, DOMAIN, AND
RP   SUBUNIT.
RX   PubMed=18424274; DOI=10.1016/j.bbapap.2008.03.009;
RA   Gutsche I., Vujicic-Zagar A., Siebert X., Servant P., Vannier F.,
RA   Castaing B., Gallet B., Heulin T., de Groot A., Sommer S., Serre L.;
RT   "Complex oligomeric structure of a truncated form of DdrA: a protein
RT   required for the extreme radiotolerance of Deinococcus.";
RL   Biochim. Biophys. Acta 1784:1050-1058(2008).
CC   -!- FUNCTION: ssDNA-binding protein that contributes to the ionizing
CC       radiation resistance of D.deserti. 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 (Probable). In vitro, binds to the 3'-ends of single-
CC       stranded DNA, and probably protects them from nuclease degradation.
CC       Thus, DdrA is part of a DNA end-protection system that helps to
CC       preserve genome integrity following irradiation or desiccation.
CC       {ECO:0000269|PubMed:18424274, ECO:0000305}.
CC   -!- SUBUNIT: The truncated form (1-160) of DdrA forms heptameric rings that
CC       can assemble into a 3-ring structure. {ECO:0000269|PubMed:18424274}.
CC   -!- INDUCTION: Induced to high levels following extreme ionizing radiation
CC       exposure. Also highly induced in response to desiccation stress (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain (1-160) is sufficient to pilot the
CC       oligomerization process and to bind specifically single-stranded DNA,
CC       but is not functional in vivo. {ECO:0000269|PubMed:18424274}.
CC   -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
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DR   EMBL; CP001114; ACO45792.1; -; Genomic_DNA.
DR   RefSeq; WP_012692915.1; NC_012526.1.
DR   AlphaFoldDB; C1D1R8; -.
DR   STRING; 546414.Deide_09150; -.
DR   PaxDb; C1D1R8; -.
DR   EnsemblBacteria; ACO45792; ACO45792; Deide_09150.
DR   KEGG; ddr:Deide_09150; -.
DR   eggNOG; COG4712; Bacteria.
DR   HOGENOM; CLU_113751_0_0_0; -.
DR   OMA; CAVQFGI; -.
DR   OrthoDB; 1614956at2; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR041247; Rad52_fam.
DR   Pfam; PF04098; Rad52_Rad22; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA-binding; Reference proteome; Stress response.
FT   CHAIN           1..201
FT                   /note="Single-stranded DNA-binding protein DdrA"
FT                   /id="PRO_0000394496"
SQ   SEQUENCE   201 AA;  22224 MW;  26BF401EA4ABF9D2 CRC64;
     MKLSDVQKRL QAPFPAHAVA WKPGVITKDR SRALMLAHID ARNVQDRLDA VCPDAWSFEV
     EVVPGTRLPT VKGRLTVLGV SREDIGEAPE GDLGTLKAAA SDALKRCAVQ FGIGRYLYDL
     PKQWVAWNDA KREPVSPPEL PEWARPDHER SPGGAHLVQA MDQLRYEMPE DLELQREVYK
     HLKAALGSLH PISGGNQGRA A